PURT_ECOLI
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 03-AUG-2022, entry version 194.
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}; OrderedLocusNames=b1849, JW1838;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 (1.75 ANGSTROMS) IN COMPLEX WITH ATP ANALOG;
RP BETA-FORMYL GLYCINAMIDE 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 (1.05 ANGSTROMS) IN COMPLEX WITH BETA-FORMYL
RP GLYCINAMIDE 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:8501063,
CC PubMed:8117714, PubMed:9184151). Catalyzes the transfer of formate to
CC 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-
CC formylglycinamide (FGAR) (PubMed:8501063, PubMed:8117714,
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=ATP + formate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide =
CC ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide +
CC phosphate; 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=ATP + carbamate = ADP + carbamoyl phosphate;
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; BAA15657.1; -; Genomic_DNA.
DR PIR; A54227; A54227.
DR RefSeq; NP_416363.1; NC_000913.3.
DR RefSeq; WP_000173484.1; NZ_SSZK01000001.1.
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 PDBsum; 1EYZ; -.
DR PDBsum; 1EZ1; -.
DR PDBsum; 1KJ8; -.
DR PDBsum; 1KJ9; -.
DR PDBsum; 1KJI; -.
DR PDBsum; 1KJJ; -.
DR PDBsum; 1KJQ; -.
DR AlphaFoldDB; P33221; -.
DR SMR; P33221; -.
DR BioGRID; 4260365; 7.
DR BioGRID; 850725; 2.
DR DIP; DIP-10618N; -.
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; P33221; -.
DR PRIDE; P33221; -.
DR EnsemblBacteria; AAC74919; AAC74919; b1849.
DR EnsemblBacteria; BAA15657; BAA15657; BAA15657.
DR GeneID; 946368; -.
DR KEGG; ecj:JW1838; -.
DR KEGG; eco:b1849; -.
DR PATRIC; fig|1411691.4.peg.400; -.
DR EchoBASE; EB1757; -.
DR eggNOG; COG0027; Bacteria.
DR InParanoid; P33221; -.
DR OMA; GMVTMIT; -.
DR PhylomeDB; P33221; -.
DR BioCyc; EcoCyc:GARTRANSFORMYL2-MON; -.
DR BioCyc; MetaCyc:GARTRANSFORMYL2-MON; -.
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; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1490.20; -; 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; IPR011054; Rudment_hybrid_motif.
DR Pfam; PF02222; ATP-grasp; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01142; purT; 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..122
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
