ID   GGPP1_ARATH             Reviewed;         371 AA.
AC   P34802; O23201;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   02-SEP-2026, entry version 176.
DE   RecName: Full=Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic;
DE            Short=GGPP synthase 1;
DE            Short=GGPS1;
DE            EC=2.5.1.-;
DE   AltName: Full=(2E,6E)-farnesyl diphosphate synthase 1;
DE   AltName: Full=Dimethylallyltranstransferase 1;
DE            EC=2.5.1.1;
DE   AltName: Full=Farnesyl diphosphate synthase 1;
DE   AltName: Full=Farnesyltranstransferase 1;
DE            EC=2.5.1.29 {ECO:0000269|PubMed:10759500};
DE   AltName: Full=Geranyltranstransferase 1;
DE            EC=2.5.1.10;
DE   Flags: Precursor;
GN   Name=GGPPS1; Synonyms=GGPPS11, GGPS1; OrderedLocusNames=At4g36810;
GN   ORFNames=C7A10.550;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8016276; DOI=10.1104/pp.104.4.1469;
RA   Scolnik P.A., Bartley G.E.;
RT   "Nucleotide sequence of an Arabidopsis cDNA for geranylgeranyl
RT   pyrophosphate synthase.";
RL   Plant Physiol. 104:1469-1470(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9461215; DOI=10.1038/35140;
RA   Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA   Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA   Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA   Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA   De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA   Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA   Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA   Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA   Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA   Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA   Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA   Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT   "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT   thaliana.";
RL   Nature 391:485-488(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=10759500; DOI=10.1104/pp.122.4.1045;
RA   Okada K., Saito T., Nakagawa T., Kawamukai M., Kamiya Y.;
RT   "Five geranylgeranyl diphosphate synthases expressed in different organs
RT   are localized into three subcellular compartments in Arabidopsis.";
RL   Plant Physiol. 122:1045-1056(2000).
RN   [7]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH GGR.
RX   PubMed=19482937; DOI=10.1073/pnas.0904069106;
RA   Wang G., Dixon R.A.;
RT   "Heterodimeric geranyl(geranyl)diphosphate synthase from hop (Humulus
RT   lupulus) and the evolution of monoterpene biosynthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9914-9919(2009).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-52, CLEAVAGE OF TRANSIT PEPTIDE
RP   [LARGE SCALE ANALYSIS] AFTER SER-51, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [9]
RP   SUBCELLULAR LOCATION, AND ALTERNATIVE INITIATION.
RX   PubMed=27707890; DOI=10.1104/pp.16.01392;
RA   Ruiz-Sola M.A., Barja M.V., Manzano D., Llorente B., Schipper B.,
RA   Beekwilder J., Rodriguez-Concepcion M.;
RT   "A single Arabidopsis gene encodes two differentially targeted
RT   geranylgeranyl diphosphate synthase isoforms.";
RL   Plant Physiol. 172:1393-1402(2016).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 72-371, AND SUBUNIT.
RX   PubMed=26537048; DOI=10.1016/j.molp.2015.10.010;
RA   Wang C., Chen Q., Fan D., Li J., Wang G., Zhang P.;
RT   "Structural analyses of short-chain prenyltransferases identify an
RT   evolutionarily conserved GFPPS clade in Brassicaceae plants.";
RL   Mol. Plant 9:195-204(2016).
CC   -!- FUNCTION: Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase
CC       large subunit. In vitro, the large subunit catalyzes mainly the trans-
CC       addition of the three molecules of IPP onto DMAPP to form
CC       geranylgeranyl pyrophosphate while the small subunit alone is inactive.
CC       Upon association of the two subunits, the product profile changes and
CC       the production of gerany-diphosphate is strongly increased.
CC       {ECO:0000269|PubMed:19482937}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=isopentenyl diphosphate + dimethylallyl diphosphate = (2E)-
CC         geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057,
CC         ChEBI:CHEBI:128769; EC=2.5.1.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=isopentenyl diphosphate + (2E)-geranyl diphosphate = (2E,6E)-
CC         farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC         ChEBI:CHEBI:175763; EC=2.5.1.10;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=isopentenyl diphosphate + (2E,6E)-farnesyl diphosphate =
CC         (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate;
CC         Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29;
CC         Evidence={ECO:0000269|PubMed:10759500};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654;
CC         Evidence={ECO:0000305|PubMed:10759500};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis;
CC       farnesyl diphosphate from geranyl diphosphate and isopentenyl
CC       diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis;
CC       geranyl diphosphate from dimethylallyl diphosphate and isopentenyl
CC       diphosphate: step 1/1.
CC   -!- PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate
CC       biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and
CC       isopentenyl diphosphate: step 1/1.
CC   -!- SUBUNIT: Forms homodimers (PubMed:26537048). Part of a heterodimeric
CC       geranyl(geranyl)diphosphate synthase. Interacts with GGR
CC       (PubMed:19482937). {ECO:0000269|PubMed:19482937,
CC       ECO:0000269|PubMed:26537048}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast
CC       {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:27707890}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:27707890}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1; Synonyms=GGPPS11 {ECO:0000303|PubMed:27707890};
CC         IsoId=P34802-1; Sequence=Displayed;
CC       Name=2; Synonyms=GGPPS11S {ECO:0000303|PubMed:27707890};
CC         IsoId=P34802-2; Sequence=VSP_062244;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC       {ECO:0000269|PubMed:10759500}.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; L25813; AAA32797.1; -; mRNA.
DR   EMBL; Z99708; CAB16803.1; -; Genomic_DNA.
DR   EMBL; AL161590; CAB80347.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86705.1; -; Genomic_DNA.
DR   EMBL; OZ408686; CAO7050170.1; -; Genomic_DNA.
DR   PIR; F85434; F85434.
DR   RefSeq; NP_195399.1; NM_119845.3. [P34802-1]
DR   PDB; 5E8L; X-ray; 2.81 A; A/B=72-371.
DR   AlphaFoldDB; P34802; -.
DR   SMR; P34802; -.
DR   BioGRID; 15115; 3.
DR   FunCoup; P34802; 251.
DR   STRING; 3702.P34802; -.
DR   iPTMnet; P34802; -.
DR   PaxDb; 3702-P34802; -.
DR   ProteomicsDB; 220742; -.
DR   GeneID; 829834; -.
DR   KEGG; ath:AT4G36810; -.
DR   Araport; AT4G36810; -.
DR   TAIR; AT4G36810; GGPS1.
DR   eggNOG; KOG0776; Eukaryota.
DR   HOGENOM; CLU_014015_0_0_1; -.
DR   InParanoid; P34802; -.
DR   OMA; AWAEFGY; -.
DR   OrthoDB; 6921389at2759; -.
DR   PhylomeDB; P34802; -.
DR   BioCyc; ARA:AT4G36810-MONOMER; -.
DR   BioCyc; MetaCyc:AT4G36810-MONOMER; -.
DR   BRENDA; 2.5.1.1; 399.
DR   BRENDA; 2.5.1.10; 399.
DR   BRENDA; 2.5.1.29; 399.
DR   UniPathway; UPA00259; UER00368.
DR   UniPathway; UPA00260; UER00369.
DR   UniPathway; UPA00389; UER00564.
DR   PRO; PR:P34802; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P34802; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; EXP:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0009513; C:etioplast; IDA:TAIR.
DR   GO; GO:0009536; C:plastid; IDA:TAIR.
DR   GO; GO:0004337; F:(2E,6E)-farnesyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004161; F:dimethylallyltranstransferase activity; IDA:TAIR.
DR   GO; GO:0004311; F:geranylgeranyl diphosphate synthase activity; IDA:TAIR.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0045337; P:farnesyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0033384; P:geranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0033386; P:geranylgeranyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; TAS:TAIR.
DR   GO; GO:0043693; P:monoterpene biosynthetic process; IMP:TAIR.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   FunFam; 1.10.600.10:FF:000001; Geranylgeranyl diphosphate synthase; 1.
DR   Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR000092; Polyprenyl_synt.
DR   InterPro; IPR033749; Polyprenyl_synt_CS.
DR   InterPro; IPR053378; Prenyl_diphosphate_synthase.
DR   NCBIfam; NF045485; FPPsyn; 1.
DR   PANTHER; PTHR43281; FARNESYL DIPHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR43281:SF32; HETERODIMERIC GERANYLGERANYL PYROPHOSPHATE SYNTHASE LARGE SUBUNIT 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00348; polyprenyl_synt; 1.
DR   SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1.
DR   SFLD; SFLDG01017; Polyprenyl_Transferase_Like; 1.
DR   SUPFAM; SSF48576; Terpenoid synthases; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
DR   PDBsum; 5E8L; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative initiation; Carotenoid biosynthesis;
KW   Chloroplast; Cytoplasm; Isoprene biosynthesis; Magnesium; Metal-binding;
KW   Plastid; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           52..371
FT                   /note="Heterodimeric geranylgeranyl pyrophosphate synthase
FT                   large subunit 1, chloroplastic"
FT                   /id="PRO_0000016471"
FT   BINDING         116
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         119
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         148
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         166
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         256
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         294
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   BINDING         321
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         52
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   VAR_SEQ         1..76
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000269|PubMed:27707890"
FT                   /id="VSP_062244"
FT   CONFLICT        108
FT                   /note="R -> S (in Ref. 1; AAA32797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        141
FT                   /note="A -> R (in Ref. 1; AAA32797)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="A -> S (in Ref. 1; AAA32797)"
FT                   /evidence="ECO:0000305"
FT   HELIX           76..94
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           101..111
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           118..129
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   TURN            134..137
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           138..155
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   TURN            158..161
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   STRAND          164..166
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           172..176
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           178..199
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   TURN            202..204
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           207..221
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   TURN            222..225
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           226..232
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           246..253
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           254..258
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           259..271
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           276..301
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   TURN            319..321
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           324..328
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           330..346
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   TURN            353..356
FT                   /evidence="ECO:0007829|PDB:5E8L"
FT   HELIX           357..368
FT                   /evidence="ECO:0007829|PDB:5E8L"
SQ   SEQUENCE   371 AA;  40174 MW;  EFA8088A75B6A005 CRC64;
     MASVTLGSWI VVHHHNHHHP SSILTKSRSR SCPITLTKPI SFRSKRTVSS SSSIVSSSVV
     TKEDNLRQSE PSSFDFMSYI ITKAELVNKA LDSAVPLREP LKIHEAMRYS LLAGGKRVRP
     VLCIAACELV GGEESTAMPA ACAVEMIHTM SLIHDDLPCM DNDDLRRGKP TNHKVFGEDV
     AVLAGDALLS FAFEHLASAT SSDVVSPVRV VRAVGELAKA IGTEGLVAGQ VVDISSEGLD
     LNDVGLEHLE FIHLHKTAAL LEASAVLGAI VGGGSDDEIE RLRKFARCIG LLFQVVDDIL
     DVTKSSKELG KTAGKDLIAD KLTYPKIMGL EKSREFAEKL NREARDQLLG FDSDKVAPLL
     ALANYIAYRQ N
//