ID   PURT_ECOLI              Reviewed;         392 AA.
AC   P33221;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2026, entry version 213.
DE   RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000305|PubMed:8117714};
DE            EC=6.3.1.21 {ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:8501063, ECO:0000269|PubMed:9184151};
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000303|PubMed:8117714};
DE   AltName: Full=Formate-dependent GAR transformylase {ECO:0000305|PubMed:8117714};
DE   AltName: Full=GAR transformylase 2 {ECO:0000303|PubMed:8117714};
DE            Short=GART 2 {ECO:0000303|PubMed:8117714};
DE   AltName: Full=GAR transformylase T {ECO:0000303|PubMed:8501063};
DE   AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000303|PubMed:8117714};
DE   AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000303|PubMed:8117714};
GN   Name=purT {ECO:0000303|PubMed:8501063};
GN   OrderedLocusNames=b1849, JW1838;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-20, FUNCTION,
RP   CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBSTRATE
RP   SPECIFICITY, REACTION MECHANISM, AND PATHWAY.
RC   STRAIN=K12;
RX   PubMed=8117714; DOI=10.1021/bi00175a023;
RA   Marolewski A., Smith J.M., Benkovic S.J.;
RT   "Cloning and characterization of a new purine biosynthetic enzyme: a non-
RT   folate glycinamide ribonucleotide transformylase from E. coli.";
RL   Biochemistry 33:2531-2537(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX   PubMed=8501063; DOI=10.1128/jb.175.11.3591-3597.1993;
RA   Nygaard P., Smith J.M.;
RT   "Evidence for a novel glycinamide ribonucleotide transformylase in
RT   Escherichia coli.";
RL   J. Bacteriol. 175:3591-3597(1993).
RN   [6]
RP   FUNCTION.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=8226647; DOI=10.1128/jb.175.21.7066-7073.1993;
RA   Nagy P.L., McCorkle G., Zalkin H.;
RT   "purU, a source of formate for purT-dependent phosphoribosyl-N-
RT   formylglycinamide synthesis.";
RL   J. Bacteriol. 175:7066-7073(1993).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP   SPECIFICITY, PATHWAY, REACTION MECHANISM, AND MUTAGENESIS OF GLY-162.
RX   PubMed=9184151; DOI=10.1021/bi962961p;
RA   Marolewski A.E., Mattia K.M., Warren M.S., Benkovic S.J.;
RT   "Formyl phosphate: a proposed intermediate in the reaction catalyzed by
RT   Escherichia coli PurT GAR transformylase.";
RL   Biochemistry 36:6709-6716(1997).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX   PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA   Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA   Grishin N.V., Zhao Y.;
RT   "Lysine acetylation is a highly abundant and evolutionarily conserved
RT   modification in Escherichia coli.";
RL   Mol. Cell. Proteomics 8:215-225(2009).
RN   [9] {ECO:0007744|PDB:1EYZ, ECO:0007744|PDB:1EZ1}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH ATP ANALOG; BETA-FORMYL GLYCINAMIDE
RP   RIBONUCLEOTIDE AND MAGNESIUM ION, AND SUBUNIT.
RX   PubMed=10913290; DOI=10.1021/bi000926j;
RA   Thoden J.B., Firestine S., Nixon A., Benkovic S.J., Holden H.M.;
RT   "Molecular structure of Escherichia coli PurT-encoded glycinamide
RT   ribonucleotide transformylase.";
RL   Biochemistry 39:8791-8802(2000).
RN   [10] {ECO:0007744|PDB:1KJ8, ECO:0007744|PDB:1KJ9, ECO:0007744|PDB:1KJI, ECO:0007744|PDB:1KJJ, ECO:0007744|PDB:1KJQ}
RP   X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH BETA-FORMYL GLYCINAMIDE
RP   RIBONUCLEOTIDE; ATP AND MAGNESIUM ION, AND SUBUNIT.
RX   PubMed=11953435; DOI=10.1074/jbc.m202251200;
RA   Thoden J.B., Firestine S.M., Benkovic S.J., Holden H.M.;
RT   "PurT-encoded glycinamide ribonucleotide transformylase. Accommodation of
RT   adenosine nucleotide analogs within the active site.";
RL   J. Biol. Chem. 277:23898-23908(2002).
CC   -!- FUNCTION: Involved in the de novo purine biosynthesis (PubMed:8117714,
CC       PubMed:8501063, PubMed:9184151). Catalyzes the transfer of formate to
CC       5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-
CC       formylglycinamide (FGAR) (PubMed:8117714, PubMed:8501063,
CC       PubMed:9184151). Formate is provided by PurU via hydrolysis of 10-
CC       formyl-tetrahydrofolate (PubMed:8226647). PurT is also able to cleave
CC       acetyl phosphate and carbamoyl phosphate to produce ATP with acetate
CC       and carbamate, respectively (PubMed:8117714, PubMed:9184151).
CC       {ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:8226647,
CC       ECO:0000269|PubMed:8501063, ECO:0000269|PubMed:9184151}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(1)-(5-phospho-beta-D-ribosyl)glycinamide + formate + ATP =
CC         N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + ADP +
CC         phosphate + H(+); Xref=Rhea:RHEA:24829, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:456216;
CC         EC=6.3.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01643,
CC         ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:8501063,
CC         ECO:0000269|PubMed:9184151};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24830;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01643,
CC         ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:8501063,
CC         ECO:0000269|PubMed:9184151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC         ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:8117714,
CC         ECO:0000269|PubMed:9184151};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamate + ATP = carbamoyl phosphate + ADP;
CC         Xref=Rhea:RHEA:30755, ChEBI:CHEBI:13941, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58228, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:9184151};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=10.1 uM for GAR (at pH 8) {ECO:0000269|PubMed:8117714,
CC         ECO:0000269|PubMed:9184151};
CC         KM=45 uM for ATP (with formate) {ECO:0000269|PubMed:9184151};
CC         KM=77.4 uM for ATP (with acetate at pH 8)
CC         {ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:9184151};
CC         KM=319 uM for formate (at pH 8) {ECO:0000269|PubMed:8117714,
CC         ECO:0000269|PubMed:9184151};
CC         KM=3.68 mM for acetate (at pH 8) {ECO:0000269|PubMed:8117714};
CC         Note=kcat is 37.6 sec(-1) for transformylase activity (at pH 8). kcat
CC         is 0.309 sec(-1) for acetate kinase activity (at pH 8).
CC         {ECO:0000269|PubMed:8117714};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-
CC       formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-
CC       ribosyl)glycinamide (formate route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01643, ECO:0000305|PubMed:8117714, ECO:0000305|PubMed:8501063,
CC       ECO:0000305|PubMed:9184151}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01643,
CC       ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435,
CC       ECO:0000305|PubMed:8117714}.
CC   -!- INTERACTION:
CC       P33221; P22939: ispA; NbExp=4; IntAct=EBI-553029, EBI-553011;
CC   -!- DISRUPTION PHENOTYPE: Mutant defective in both purN and purT requires
CC       an exogenous purine source for growth. {ECO:0000269|PubMed:8501063}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
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DR   EMBL; L20897; AAA23861.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74919.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15657.2; -; Genomic_DNA.
DR   PIR; A54227; A54227.
DR   RefSeq; NP_416363.1; NC_000913.3.
DR   RefSeq; WP_000173484.1; NZ_CP009789.1.
DR   PDB; 1EYZ; X-ray; 1.75 A; A/B=1-392.
DR   PDB; 1EZ1; X-ray; 1.75 A; A/B=1-392.
DR   PDB; 1KJ8; X-ray; 1.60 A; A/B=2-392.
DR   PDB; 1KJ9; X-ray; 1.60 A; A/B=2-392.
DR   PDB; 1KJI; X-ray; 1.60 A; A/B=2-392.
DR   PDB; 1KJJ; X-ray; 1.75 A; A/B=2-392.
DR   PDB; 1KJQ; X-ray; 1.05 A; A/B=2-392.
DR   AlphaFoldDB; P33221; -.
DR   SMR; P33221; -.
DR   BioGRID; 4260365; 14.
DR   BioGRID; 850725; 7.
DR   DIP; DIP-10618N; -.
DR   FunCoup; P33221; 184.
DR   IntAct; P33221; 7.
DR   STRING; 511145.b1849; -.
DR   DrugBank; DB03434; 3-(N-morpholino)propanesulfonic acid.
DR   DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate.
DR   DrugBank; DB03909; Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate.
DR   DrugBank; DB02236; Glycinamide Ribonucleotide.
DR   DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR   iPTMnet; P33221; -.
DR   jPOST; P33221; -.
DR   PaxDb; 511145-b1849; -.
DR   EnsemblBacteria; AAC74919; AAC74919; b1849.
DR   GeneID; 93776116; -.
DR   GeneID; 946368; -.
DR   KEGG; ecj:JW1838; -.
DR   KEGG; eco:b1849; -.
DR   KEGG; ecoc:C3026_10535; -.
DR   PATRIC; fig|1411691.4.peg.400; -.
DR   EchoBASE; EB1757; -.
DR   eggNOG; COG0027; Bacteria.
DR   InParanoid; P33221; -.
DR   OMA; AADMERC; -.
DR   OrthoDB; 9804625at2; -.
DR   PhylomeDB; P33221; -.
DR   BioCyc; EcoCyc:GARTRANSFORMYL2-MONOMER; -.
DR   BioCyc; MetaCyc:GARTRANSFORMYL2-MONOMER; -.
DR   BRENDA; 6.3.1.21; 2026.
DR   SABIO-RK; P33221; -.
DR   UniPathway; UPA00074; UER00127.
DR   EvolutionaryTrace; P33221; -.
DR   PHI-base; PHI:8653; -.
DR   PRO; PR:P33221; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P33221; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0008776; F:acetate kinase activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; EXP:UniProtKB.
DR   GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   FunFam; 3.30.1490.20:FF:000013; Formate-dependent phosphoribosylglycinamide formyltransferase; 1.
DR   FunFam; 3.30.470.20:FF:000027; Formate-dependent phosphoribosylglycinamide formyltransferase; 1.
DR   FunFam; 3.40.50.20:FF:000007; Formate-dependent phosphoribosylglycinamide formyltransferase; 1.
DR   Gene3D; 3.40.50.20; -; 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   HAMAP; MF_01643; PurT; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR003135; ATP-grasp_carboxylate-amine.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR005862; PurT.
DR   InterPro; IPR054350; PurT/PurK_preATP-grasp.
DR   InterPro; IPR048740; PurT_C.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   NCBIfam; NF006766; purT; 1.
DR   NCBIfam; TIGR01142; purT; 1.
DR   PANTHER; PTHR43055; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR43055:SF1; FORMATE-DEPENDENT PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   Pfam; PF02222; ATP-grasp; 1.
DR   Pfam; PF21244; PurT_C; 1.
DR   Pfam; PF22660; RS_preATP-grasp-like; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Direct protein sequencing; Ligase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8117714"
FT   CHAIN           2..392
FT                   /note="Formate-dependent phosphoribosylglycinamide
FT                   formyltransferase"
FT                   /id="PRO_0000074956"
FT   DOMAIN          119..308
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         22..23
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         82
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         155
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         160..165
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         195..198
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         267
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         286
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         355
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   BINDING         362..363
FT                   /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT                   /ligand_id="ChEBI:CHEBI:143788"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643,
FT                   ECO:0000269|PubMed:10913290, ECO:0000269|PubMed:11953435"
FT   MOD_RES         179
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:18723842"
FT   MUTAGEN         162
FT                   /note="G->I: Strong decrease in the reaction rate for the
FT                   conversion of formate to FGAR and in the affinity for
FT                   formate. 3- and 2-fold decrease in the affinity for ATP and
FT                   GAR, respectively."
FT                   /evidence="ECO:0000269|PubMed:9184151"
FT   STRAND          14..19
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           22..32
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   TURN            33..35
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          37..44
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           48..52
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          53..58
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           88..96
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          100..103
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           105..112
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           114..119
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           120..124
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           138..148
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          150..157
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   TURN            161..164
FT                   /evidence="ECO:0007829|PDB:1KJ8"
FT   STRAND          166..168
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           174..184
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           186..188
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          192..196
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          201..211
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          214..217
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          221..226
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          229..235
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           241..258
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          260..271
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          274..283
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           286..290
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           291..294
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          295..297
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           299..307
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          319..326
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          329..334
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          336..338
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           340..342
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          348..352
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          358..361
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          365..370
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   HELIX           374..387
FT                   /evidence="ECO:0007829|PDB:1KJQ"
FT   STRAND          389..391
FT                   /evidence="ECO:0007829|PDB:1KJQ"
SQ   SEQUENCE   392 AA;  42434 MW;  276B3883E7403EA9 CRC64;
     MTLLGTALRP AATRVMLLGS GELGKEVAIE CQRLGVEVIA VDRYADAPAM HVAHRSHVIN
     MLDGDALRRV VELEKPHYIV PEIEAIATDM LIQLEEEGLN VVPCARATKL TMNREGIRRL
     AAEELQLPTS TYRFADSESL FREAVADIGY PCIVKPVMSS SGKGQTFIRS AEQLAQAWKY
     AQQGGRAGAG RVIVEGVVKF DFEITLLTVS AVDGVHFCAP VGHRQEDGDY RESWQPQQMS
     PLALERAQEI ARKVVLALGG YGLFGVELFV CGDEVIFSEV SPRPHDTGMV TLISQDLSEF
     ALHVRAFLGL PVGGIRQYGP AASAVILPQL TSQNVTFDNV QNAVGADLQI RLFGKPEIDG
     SRRLGVALAT AESVVDAIER AKHAAGQVKV QG
//