ID   PPDK1_MAIZE             Reviewed;         947 AA.
AC   P11155; C5IHE0; Q41846; Q41847; Q42367; Q7DMU6; Q9XGW9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   02-SEP-2026, entry version 176.
DE   RecName: Full=Pyruvate, phosphate dikinase 1, chloroplastic {ECO:0000303|PubMed:1668653};
DE            EC=2.7.9.1 {ECO:0000269|PubMed:10683263, ECO:0000269|PubMed:21414960, ECO:0000269|PubMed:9038349, ECO:0000269|PubMed:9287137};
DE   AltName: Full=Pyruvate, orthophosphate dikinase 1;
DE   Flags: Precursor;
GN   Name=PPDK1 {ECO:0000303|PubMed:1668653};
GN   Synonyms=C4PPDKZM1 {ECO:0000303|PubMed:1668653}, CYPPDKZM1
GN   {ECO:0000303|PubMed:1668653}, PPDK2 {ECO:0000303|PubMed:2158100};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C4PPDKZM1), AND PROTEIN SEQUENCE OF
RP   71-89.
RX   PubMed=2841317; DOI=10.1016/s0021-9258(18)37924-9;
RA   Matsuoka M., Ozeki Y., Yamamoto N., Hirano H., Kano-Murakami Y., Tanaka Y.;
RT   "Primary structure of maize pyruvate, orthophosphate dikinase as deduced
RT   from cDNA sequence.";
RL   J. Biol. Chem. 263:11080-11083(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2170354; DOI=10.1016/s0021-9258(17)44827-7;
RA   Matsuoka M.;
RT   "Structure, genetic mapping, and expression of the gene for pyruvate,
RT   orthophosphate dikinase from maize.";
RL   J. Biol. Chem. 265:16772-16777(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CYPPDKZM1).
RC   STRAIN=cv. LH52;
RX   PubMed=19329568; DOI=10.1104/pp.108.131888;
RA   Manicacci D., Camus-Kulandaivelu L., Fourmann M., Arar C., Barrault S.,
RA   Rousselet A., Feminias N., Consoli L., Frances L., Mechin V., Murigneux A.,
RA   Prioul J.L., Charcosset A., Damerval C.;
RT   "Epistatic interactions between Opaque2 transcriptional activator and its
RT   target gene CyPPDK1 control kernel trait variation in maize.";
RL   Plant Physiol. 150:506-520(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-75 (ISOFORM C4PPDKZM1), ALTERNATIVE
RP   PROMOTER USAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. B73;
RX   PubMed=2158100; DOI=10.1073/pnas.87.8.3004;
RA   Glackin C.A., Grula J.W.;
RT   "Organ-specific transcripts of different size and abundance derive from the
RT   same pyruvate, orthophosphate dikinase gene in maize.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:3004-3008(1990).
RN   [5]
RP   PROTEIN SEQUENCE OF 521-535, AND PHOSPHORYLATION AT THR-527.
RX   PubMed=2834385; DOI=10.1016/s0021-9258(18)68696-x;
RA   Roeske C.A., Kutny R.M., Budde R.J.A., Chollet R.;
RT   "Sequence of the phosphothreonyl regulatory site peptide from inactive
RT   maize leaf pyruvate, orthophosphate dikinase.";
RL   J. Biol. Chem. 263:6683-6687(1988).
RN   [6]
RP   PROTEIN SEQUENCE OF 524-535, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
RP   THR-527.
RC   STRAIN=cv. Olenka; TISSUE=Bundle sheath cell, and Mesophyll cell;
RX   PubMed=22833285; DOI=10.1002/pmic.201200196;
RA   Fristedt R., Wasilewska W., Romanowska E., Vener A.V.;
RT   "Differential phosphorylation of thylakoid proteins in mesophyll and bundle
RT   sheath chloroplasts from maize plants grown under low or high light.";
RL   Proteomics 12:2852-2861(2012).
RN   [7]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C4PPDKZM1 AND CYPPDKZM1),
RP   MUTAGENESIS OF GLY-525 AND SER-528, ALTERNATIVE PROMOTER USAGE, FUNCTION,
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP   INDUCTION.
RX   PubMed=1668653; DOI=10.1105/tpc.3.3.225;
RA   Sheen J.;
RT   "Molecular mechanisms underlying the differential expression of maize
RT   pyruvate, orthophosphate dikinase genes.";
RL   Plant Cell 3:225-245(1991).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 868-947.
RC   STRAIN=cv. B73;
RA   Stapleton A.E., Walbot V.;
RT   "Maize clones with putative DNA-binding activity.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PROTEIN SEQUENCE OF 63-74, IDENTIFICATION BY MASS SPECTROMETRY,
RP   PHOSPHORYLATION AT THR-309; SER-506; THR-527 AND SER-528, TISSUE
RP   SPECIFICITY, INDUCTION BY LIGHT, ACETYLATION AT ALA-63, AND CLEAVAGE OF
RP   INITIATOR METHIONINE (ISOFORM CYPPDKZM1).
RX   PubMed=24710069; DOI=10.1104/pp.113.231993;
RA   Chen Y.B., Lu T.C., Wang H.X., Shen J., Bu T.T., Chao Q., Gao Z.F.,
RA   Zhu X.G., Wang Y.F., Wang B.C.;
RT   "Posttranslational modification of maize chloroplast pyruvate
RT   orthophosphate dikinase reveals the precise regulatory mechanism of its
RT   enzymatic activity.";
RL   Plant Physiol. 165:534-549(2014).
RN   [10]
RP   ACTIVITY REGULATION.
RX   PubMed=16660615; DOI=10.1104/pp.62.5.826;
RA   Shirahashi K., Hayakawa S., Sugiyama T.;
RT   "Cold lability of pyruvate, orthophosphate dikinase in the Maize Leaf.";
RL   Plant Physiol. 62:826-830(1978).
RN   [11]
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP   MUTAGENESIS OF LEU-946.
RX   PubMed=9038349; DOI=10.1016/s0014-5793(97)00015-x;
RA   Ohta S., Usami S., Ueki J., Kumashiro T., Komari T., Burnell J.N.;
RT   "Identification of the amino acid residues responsible for cold tolerance
RT   in Flaveria brownii pyruvate,orthophosphate dikinase.";
RL   FEBS Lett. 403:5-9(1997).
RN   [12]
RP   CATALYTIC ACTIVITY, MUTAGENESIS OF THR-527, AND COFACTOR.
RX   PubMed=9287137; DOI=10.1016/s0014-5793(97)00884-3;
RA   Chastain C.J., Lee M.E., Moorman M.A., Shameekumar P., Chollet R.;
RT   "Site-directed mutagenesis of maize recombinant C4-pyruvate,orthophosphate
RT   dikinase at the phosphorylatable target threonine residue.";
RL   FEBS Lett. 413:169-173(1997).
RN   [13]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACTIVE SITE HIS-529, AND
RP   MUTAGENESIS OF THR-527 AND HIS-529.
RX   PubMed=10683263; DOI=10.1006/abbi.1999.1651;
RA   Chastain C.J., Botschner M., Harrington G.E., Thompson B.J., Mills S.E.,
RA   Sarath G., Chollet R.;
RT   "Further analysis of maize C(4) pyruvate,orthophosphate dikinase
RT   phosphorylation by its bifunctional regulatory protein using selective
RT   substitutions of the regulatory Thr-456 and catalytic His-458 residues.";
RL   Arch. Biochem. Biophys. 375:165-170(2000).
RN   [14]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=21414960; DOI=10.1093/jxb/err058;
RA   Chastain C.J., Failing C.J., Manandhar L., Zimmerman M.A., Lakner M.M.,
RA   Nguyen T.H.;
RT   "Functional evolution of C(4) pyruvate, orthophosphate dikinase.";
RL   J. Exp. Bot. 62:3083-3091(2011).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 72-947 IN APOPROTEIN AND IN
RP   COMPLEX WITH SUBSTRATE, ACTIVE SITE CYS-907, METAL BINDING AT GLU-821 AND
RP   ASP-845, AND SUBSTRATE BINDING AT ARG-635; ARG-692; ASN-844 AND ASP-845.
RX   PubMed=15667207; DOI=10.1021/bi0484522;
RA   Nakanishi T., Nakatsu T., Matsuoka M., Sakata K., Kato H.;
RT   "Crystal structures of pyruvate phosphate dikinase from maize revealed an
RT   alternative conformation in the swiveling-domain motion.";
RL   Biochemistry 44:1136-1144(2005).
CC   -!- FUNCTION: Formation of phosphoenolpyruvate, which is the primary
CC       acceptor of CO(2) in C4 and some Crassulacean acid metabolism plants.
CC       {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:21414960}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=pyruvate + phosphate + ATP = phosphoenolpyruvate + AMP +
CC         diphosphate + H(+); Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC         Evidence={ECO:0000269|PubMed:10683263, ECO:0000269|PubMed:21414960,
CC         ECO:0000269|PubMed:9038349};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:15667207, ECO:0000305|PubMed:9287137};
CC   -!- ACTIVITY REGULATION: Activated by light-induced dephosphorylation.
CC       Inhibited by dark-induced phosphorylation. Both reactions are catalyzed
CC       by PDRP1. Inactivated by cold due to the dissociation of the
CC       homotetramer. Independent of circadian regulation (PubMed:24710069).
CC       {ECO:0000269|PubMed:10683263, ECO:0000269|PubMed:16660615,
CC       ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:9038349}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=158 uM for pyruvate {ECO:0000269|PubMed:9038349};
CC         KM=178 uM for pyruvate {ECO:0000269|PubMed:21414960};
CC         KM=95 uM for ATP {ECO:0000269|PubMed:9038349};
CC         KM=194 uM for phosphoenolpyruvate {ECO:0000269|PubMed:21414960};
CC         KM=408 uM for phosphate {ECO:0000269|PubMed:9038349};
CC       Temperature dependence:
CC         Loss of activity below 10 degrees Celsius.
CC         {ECO:0000269|PubMed:9038349};
CC   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15667207}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:1668653,
CC       ECO:0000269|PubMed:22833285}. Cytoplasm {ECO:0000269|PubMed:1668653}.
CC       Note=Isoform C4PPDKZM1 is targeted to the chloroplast while isoform
CC       CYPPDKZM1 is found in the cytoplasm. Can be found associated with the
CC       thylakoid membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=C4PPDKZM1 {ECO:0000303|PubMed:1668653}; Synonyms=C4PPDK
CC       {ECO:0000303|PubMed:24710069};
CC         IsoId=P11155-1; Sequence=Displayed;
CC       Name=CYPPDKZM1 {ECO:0000303|PubMed:1668653,
CC       ECO:0000303|PubMed:24710069};
CC         IsoId=P11155-2; Sequence=VSP_057373;
CC   -!- TISSUE SPECIFICITY: Isoform C4PPDKZM1 mainly localized in mesophyll
CC       cells and only a low level is found in bundle sheath cells. Isoform
CC       CYPPDKZM1 expressed in roots, stems and etiolated leaves.
CC       {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:2158100,
CC       ECO:0000269|PubMed:24710069}.
CC   -!- INDUCTION: Isoform C4ppdkZm1 is light-inducible.
CC       {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:24710069}.
CC   -!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site, the
CC       central domain the pyrophosphate/phosphate carrier histidine, and the
CC       C-terminal domain the pyruvate binding site.
CC   -!- PTM: Phosphorylation of Thr-527 in the dark inactivates the enzyme,
CC       dephosphorylation upon light stimulation reactivates the enzyme
CC       (PubMed:2834385). More highly phosphorylated when grown under high
CC       rather than low light regimes (70 vs 900 umol photons/m-2/s). the
CC       degree of phosphorylation is strictly regulated by light intensity and
CC       the light/dark transition has no influence (PubMed:24710069).
CC       Phosphorylated in both mesophyll and bundle sheath cells
CC       (PubMed:22833285). The phosphorylation at Ser-528 may be important for
CC       the phosphorylation at Thr-527 and may also be regulated by light
CC       intensity (PubMed:24710069). {ECO:0000269|PubMed:22833285,
CC       ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:2834385}.
CC   -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC       phosphocarrier histidine residue located on the surface of the central
CC       domain. The two first partial reactions are catalyzed at an active site
CC       located on the N-terminal domain, and the third partial reaction is
CC       catalyzed at an active site located on the C-terminal domain. For
CC       catalytic turnover, the central domain swivels from the concave surface
CC       of the N-terminal domain to that of the C-terminal domain.
CC   -!- MISCELLANEOUS: PubMed:1668653 shows the existence of a second gene
CC       coding only for the short cytoplasmic isoform of PPDK.
CC   -!- MISCELLANEOUS: [Isoform CYPPDKZM1]: Produced by alternative promoter
CC       usage (PubMed:1668653). Cytoplasmic (PubMed:1668653). Initiator Met-1
CC       is removed (PubMed:24710069). {ECO:0000269|PubMed:1668653,
CC       ECO:0000269|PubMed:24710069}.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33495.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; J03901; AAA33495.1; ALT_FRAME; mRNA.
DR   EMBL; M58656; AAA33498.1; -; Genomic_DNA.
DR   EMBL; M58655; AAA33498.1; JOINED; Genomic_DNA.
DR   EMBL; S46966; AAB23731.1; -; Genomic_DNA.
DR   EMBL; S46965; AAB23730.1; -; Genomic_DNA.
DR   EMBL; S46964; AAB23730.1; JOINED; Genomic_DNA.
DR   EMBL; X14927; CAA33054.1; -; Genomic_DNA.
DR   EMBL; FJ935764; ACR78549.1; -; Genomic_DNA.
DR   EMBL; AF152599; AAD45281.1; -; mRNA.
DR   PIR; A29225; KIZMPO.
DR   PIR; PQ0190; PQ0190.
DR   PDB; 1VBG; X-ray; 2.30 A; A=72-947.
DR   PDB; 1VBH; X-ray; 2.30 A; A=72-947.
DR   AlphaFoldDB; P11155; -.
DR   SMR; P11155; -.
DR   FunCoup; P11155; 489.
DR   STRING; 4577.P11155; -.
DR   iPTMnet; P11155; -.
DR   PaxDb; 4577-P11155; -.
DR   MaizeGDB; 25385; -.
DR   InParanoid; P11155; -.
DR   BRENDA; 2.7.9.1; 6752.
DR   SABIO-RK; P11155; -.
DR   UniPathway; UPA00322; -.
DR   EvolutionaryTrace; P11155; -.
DR   Proteomes; UP000007305; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:InterPro.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; EXP:UniProtKB.
DR   FunFam; 3.20.20.60:FF:000040; Pyruvate, phosphate dikinase, chloroplastic; 1.
DR   FunFam; 3.30.470.20:FF:000038; Pyruvate, phosphate dikinase, chloroplastic; 1.
DR   FunFam; 3.50.30.10:FF:000009; Pyruvate, phosphate dikinase, chloroplastic; 1.
DR   Gene3D; 1.20.80.30; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR   Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR   Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR   InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_kinase-like_dom_sf.
DR   NCBIfam; NF004531; PRK05878.1; 1.
DR   NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR   PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR   PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF01326; PPDK_N; 3.
DR   PIRSF; PIRSF000853; PPDK; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
DR   PDBsum; 1VBG; -.
DR   PDBsum; 1VBH; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative promoter usage; ATP-binding;
KW   Chloroplast; Cytoplasm; Direct protein sequencing; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Photosynthesis; Plastid;
KW   Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..62
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:24710069"
FT   CHAIN           63..947
FT                   /note="Pyruvate, phosphate dikinase 1, chloroplastic"
FT                   /id="PRO_0000431714"
FT   REGION          21..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        529
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000269|PubMed:10683263"
FT   ACT_SITE        907
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:15667207"
FT   BINDING         635
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15667207"
FT   BINDING         692
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15667207"
FT   BINDING         821
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:15667207"
FT   BINDING         821
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15667207"
FT   BINDING         842
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15667207"
FT   BINDING         843
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15667207"
FT   BINDING         844
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15667207"
FT   BINDING         845
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:15667207"
FT   BINDING         845
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:15667207"
FT   MOD_RES         63
FT                   /note="N-acetylalanine; partial"
FT                   /evidence="ECO:0000269|PubMed:24710069"
FT   MOD_RES         309
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:24710069"
FT   MOD_RES         506
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:24710069"
FT   MOD_RES         527
FT                   /note="Phosphothreonine; by PDRP1"
FT                   /evidence="ECO:0000269|PubMed:22833285,
FT                   ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:2834385"
FT   MOD_RES         528
FT                   /note="Phosphoserine; by PDRP1"
FT                   /evidence="ECO:0000269|PubMed:24710069"
FT   VAR_SEQ         1..75
FT                   /note="MAASVSRAICVQKPGSKCTRDREATSFARRSVAAPRPPHAKAAGVIRSDSGA
FT                   GRGQHCSPLRAVVDAAPIQTTKK -> MAPVQCARSQ (in isoform
FT                   CYPPDKZM1)"
FT                   /id="VSP_057373"
FT   MUTAGEN         525
FT                   /note="G->A,P: Greatly reduced activity. Strongly reduced
FT                   or lack of phosphorylation by PDRP1 in vitro."
FT                   /evidence="ECO:0000269|PubMed:24710069"
FT   MUTAGEN         527
FT                   /note="T->D,E: Abolished activity."
FT                   /evidence="ECO:0000269|PubMed:10683263,
FT                   ECO:0000269|PubMed:9287137"
FT   MUTAGEN         527
FT                   /note="T->N: Greatly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:10683263,
FT                   ECO:0000269|PubMed:9287137"
FT   MUTAGEN         527
FT                   /note="T->S,V: No effect on activity."
FT                   /evidence="ECO:0000269|PubMed:10683263,
FT                   ECO:0000269|PubMed:9287137"
FT   MUTAGEN         527
FT                   /note="T->Y: Greatly reduced activity. No tyrosine
FT                   phosphorylation by PDRP1 in vitro."
FT                   /evidence="ECO:0000269|PubMed:10683263,
FT                   ECO:0000269|PubMed:9287137"
FT   MUTAGEN         528
FT                   /note="S->C: No effect on activity or phosphorylation by
FT                   PDRP1 in vitro."
FT                   /evidence="ECO:0000269|PubMed:24710069"
FT   MUTAGEN         528
FT                   /note="S->Y,T: Greatly reduced activity. Strongly reduced
FT                   or lack of phosphorylation by PDRP1 in vitro."
FT                   /evidence="ECO:0000269|PubMed:24710069"
FT   MUTAGEN         529
FT                   /note="H->N: Abolished activity. No phosphorylation on
FT                   T-527 by PDRP1 in vitro."
FT                   /evidence="ECO:0000269|PubMed:10683263"
FT   MUTAGEN         946
FT                   /note="L->V: No decrease of the cold sensitivity."
FT                   /evidence="ECO:0000269|PubMed:9038349"
FT   CONFLICT        2
FT                   /note="A -> T (in Ref. 2; AAA33498 and 7; AAB23730)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="Missing (in Ref. 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        404
FT                   /note="R -> G (in Ref. 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        536
FT                   /note="W -> G (in Ref. 2; AAA33498 and 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        561
FT                   /note="S -> G (in Ref. 2; AAA33498 and 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        671
FT                   /note="T -> P (in Ref. 2; AAA33498 and 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        696..699
FT                   /note="HPSY -> PPLH (in Ref. 2; AAA33498 and 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        760
FT                   /note="A -> V (in Ref. 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        865
FT                   /note="H -> Y (in Ref. 2; AAA33498 and 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        869..873
FT                   /note="GILQH -> EFGTS (in Ref. 8; AAD45281)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        878
FT                   /note="V -> I (in Ref. 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        890
FT                   /note="F -> L (in Ref. 2; AAA33498 and 3; ACR78549)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        927
FT                   /note="F -> Y (in Ref. 2; AAA33498, 8; AAD45281 and 3;
FT                   ACR78549)"
FT                   /evidence="ECO:0000305"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            92..95
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           96..107
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          115..118
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           120..128
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:1VBH"
FT   HELIX           137..152
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          159..162
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          165..168
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           178..181
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           189..199
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           201..218
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           224..238
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           243..245
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           248..266
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           274..288
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           292..299
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            300..302
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          311..315
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          326..333
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            335..337
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          343..350
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           352..357
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           366..371
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           373..390
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          394..401
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          404..412
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           417..429
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           435..438
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           439..441
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           444..449
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          454..456
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           458..461
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            462..464
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          465..468
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          470..473
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          475..484
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           485..493
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          498..503
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            507..509
FT                   /evidence="ECO:0007829|PDB:1VBH"
FT   HELIX           510..515
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          516..523
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           529..536
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          541..543
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          548..551
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           552..554
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          556..559
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          562..565
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          569..573
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            574..577
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          578..582
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           587..590
FT                   /evidence="ECO:0007829|PDB:1VBH"
FT   HELIX           593..605
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          608..613
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           617..625
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          630..635
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           636..640
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           644..655
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           659..683
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            684..686
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          687..692
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           698..701
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           707..718
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           722..732
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           737..739
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           744..749
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           751..769
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            770..772
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          776..781
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           787..808
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          815..820
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           823..827
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           829..832
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            833..835
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          837..841
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           843..851
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            855..857
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           858..860
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           862..867
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            875..877
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   TURN            881..883
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           884..898
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          903..908
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           909..912
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           914..922
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   STRAND          926..930
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           932..934
FT                   /evidence="ECO:0007829|PDB:1VBG"
FT   HELIX           935..944
FT                   /evidence="ECO:0007829|PDB:1VBG"
SQ   SEQUENCE   947 AA;  102674 MW;  6D11F51D150ACFD1 CRC64;
     MAASVSRAIC VQKPGSKCTR DREATSFARR SVAAPRPPHA KAAGVIRSDS GAGRGQHCSP
     LRAVVDAAPI QTTKKRVFHF GKGKSEGNKT MKELLGGKGA NLAEMASIGL SVPPGFTVST
     EACQQYQDAG CALPAGLWAE IVDGLQWVEE YMGATLGDPQ RPLLLSVRSG AAVSMPGMMD
     TVLNLGLNDE VAAGLAAKSG ERFAYDSFRR FLDMFGNVVM DIPRSLFEEK LEHMKESKGL
     KNDTDLTASD LKELVGQYKE VYLSAKGEPF PSDPKKQLEL AVLAVFNSWE SPRAKKYRSI
     NQITGLRGTA VNVQCMVFGN MGNTSGTGVL FTRNPNTGEK KLYGEFLVNA QGEDVVAGIR
     TPEDLDAMKN LMPQAYDELV ENCNILESHY KEMQDIEFTV QENRLWMLQC RTGKRTGKSA
     VKIAVDMVNE GLVEPRSAIK MVEPGHLDQL LHPQFENPSA YKDQVIATGL PASPGAAVGQ
     VVFTAEDAEA WHSQGKAAIL VRAETSPEDV GGMHAAVGIL TERGGMTSHA AVVARWWGKC
     CVSGCSGIRV NDAEKLVTIG SHVLREGEWL SLNGSTGEVI LGKQPLSPPA LSGDLGTFMA
     WVDDVRKLKV LANADTPDDA LTARNNGAQG IGLCRTEHMF FASDERIKAV RQMIMAPTLE
     LRQQALDRLL TYQRSDFEGI FRAMDGLPVT IRLLDHPSYE FLPEGNIEDI VSELCAETGA
     NQEDALARIE KLSEVNPMLG FRGCRLGISY PELTEMQARA IFEAAIAMTN QGVQVFPEIM
     VPLVGTPQEL GHQVTLIRQV AEKVFANVGK TIGYKVGTMI EIPRAALVAD EIAEQAEFFS
     FGTNDLTQMT FGYSRDDVGK FIPVHLAQGI LQHDPFEVLD QRGVGELVKF ATERGRKARP
     NLKVGICGEH GGEPSSVAFF AKAGLDFVSC SPFRVPIARL AAAQVLV
//