ID   PUR1_ECOLI              Reviewed;         505 AA.
AC   P0AG16; P00496; P78092; P78191; P78192; Q47255; Q59425;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000303|PubMed:6443594};
DE            Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE            EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000269|PubMed:372191};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000303|PubMed:372191};
DE            Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931, ECO:0000303|PubMed:9333323};
GN   Name=purF {ECO:0000255|HAMAP-Rule:MF_01931};
GN   OrderedLocusNames=b2312, JW2309;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1] {ECO:0000312|EMBL:CAA30971.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3047685; DOI=10.1093/nar/16.17.8717;
RA   Sampei G., Mizobuchi K.;
RT   "Nucleotide sequence of the Escherichia coli purF gene encoding
RT   amidophosphoribosyltransferase for de novo purine nucleotide synthesis.";
RL   Nucleic Acids Res. 16:8717-8717(1988).
RN   [2] {ECO:0000312|EMBL:AAA24453.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6443594; DOI=10.1016/0065-2571(83)90016-x;
RA   Zalkin H.;
RT   "Structure, function, and regulation of amidophosphoribosyltransferase from
RT   prokaryotes.";
RL   Adv. Enzyme Regul. 21:225-237(1983).
RN   [3] {ECO:0000312|EMBL:AAA24452.1, ECO:0000312|EMBL:CAA23613.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6277938; DOI=10.1016/s0021-9258(18)34810-5;
RA   Tso J.Y., Zalkin H., van Cleemput M., Yanofsky C., Smith J.M.;
RT   "Nucleotide sequence of Escherichia coli purF and deduced amino acid
RT   sequence of glutamine phosphoribosylpyrophosphate amidotransferase.";
RL   J. Biol. Chem. 257:3525-3531(1982).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [5] {ECO:0000312|EMBL:AAC75372.1}
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   [6] {ECO:0000312|EMBL:BAA16158.2}
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   [7] {ECO:0000312|EMBL:AAA23969.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31 AND 483-505.
RC   STRAIN=K12;
RX   PubMed=3040734; DOI=10.1016/s0021-9258(18)45338-0;
RA   Nonet M.L., Marvel C.C., Tolan D.R.;
RT   "The hisT-purF region of the Escherichia coli K-12 chromosome.
RT   Identification of additional genes of the hisT and purF operons.";
RL   J. Biol. Chem. 262:12209-12217(1987).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-24, AND ACTIVE SITE.
RX   PubMed=7037784; DOI=10.1016/s0021-9258(18)34811-7;
RA   Tso J.Y., Hermodson M.A., Zalkin H.;
RT   "Glutamine phosphoribosylpyrophosphate amidotransferase from cloned
RT   Escherichia coli purF. NH2-terminal amino acid sequence, identification of
RT   the glutamine site, and trace metal analysis.";
RL   J. Biol. Chem. 257:3532-3536(1982).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND PATHWAY.
RX   PubMed=372191; DOI=10.1016/s0021-9258(18)50771-7;
RA   Messenger L.J., Zalkin H.;
RT   "Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia
RT   coli. Purification and properties.";
RL   J. Biol. Chem. 254:3382-3392(1979).
RN   [10]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=9333323; DOI=10.1021/bi9714114;
RA   Krahn J.M., Kim J.H., Burns M.R., Parry R.J., Zalkin H., Smith J.L.;
RT   "Coupled formation of an amidotransferase interdomain ammonia channel and a
RT   phosphoribosyltransferase active site.";
RL   Biochemistry 36:11061-11068(1997).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX   PubMed=9514258; DOI=10.1002/pro.5560070104;
RA   Muchmore C.R.A., Krahn J.M., Kim J.H., Zalkin H., Smith J.L.;
RT   "Crystal structure of glutamine phosphoribosylpyrophosphate
RT   amidotransferase from Escherichia coli.";
RL   Protein Sci. 7:39-51(1998).
CC   -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC       phosphoribosylpyrophosphate (PRPP) and glutamine. Can also use NH(3) in
CC       place of glutamine. {ECO:0000269|PubMed:372191}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC         Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01931, ECO:0000269|PubMed:372191};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01931};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931};
CC   -!- ACTIVITY REGULATION: Inhibited by iodoacetamide and by the glutamine
CC       analogs chloroketone and DON. {ECO:0000269|PubMed:372191}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.067 mM for phosphoribosylpyrophosphate
CC         {ECO:0000269|PubMed:372191};
CC         KM=1.7 mM for glutamine {ECO:0000269|PubMed:372191};
CC         KM=8.8 mM for NH(3) {ECO:0000269|PubMed:372191};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC       (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC       diphosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01931,
CC       ECO:0000269|PubMed:372191}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:9514258}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01931,
CC       ECO:0000305}.
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DR   EMBL; X12423; CAA30971.1; -; Genomic_DNA.
DR   EMBL; V00322; CAA23613.1; -; Genomic_DNA.
DR   EMBL; M26893; AAA24453.1; -; Genomic_DNA.
DR   EMBL; J01666; AAA24452.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75372.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16158.2; -; Genomic_DNA.
DR   EMBL; AH000881; AAA23969.1; ALT_SEQ; Genomic_DNA.
DR   PIR; F65003; XQEC.
DR   RefSeq; NP_416815.1; NC_000913.3.
DR   RefSeq; WP_000334220.1; NZ_STEB01000008.1.
DR   PDB; 1ECB; X-ray; 2.70 A; A/B/C/D=2-505.
DR   PDB; 1ECC; X-ray; 2.40 A; A/B=2-505.
DR   PDB; 1ECF; X-ray; 2.00 A; A/B=2-505.
DR   PDB; 1ECG; X-ray; 2.30 A; A/B=2-505.
DR   PDB; 1ECJ; X-ray; 2.50 A; A/B/C/D=2-505.
DR   PDB; 6CZF; X-ray; 1.95 A; A/B/C/D=2-499.
DR   PDB; 6OTT; X-ray; 2.55 A; A/B=2-505.
DR   PDBsum; 1ECB; -.
DR   PDBsum; 1ECC; -.
DR   PDBsum; 1ECF; -.
DR   PDBsum; 1ECG; -.
DR   PDBsum; 1ECJ; -.
DR   PDBsum; 6CZF; -.
DR   PDBsum; 6OTT; -.
DR   AlphaFoldDB; P0AG16; -.
DR   SMR; P0AG16; -.
DR   BioGRID; 4261075; 7.
DR   STRING; 511145.b2312; -.
DR   DrugBank; DB04296; 5-Oxo-L-Norleucine.
DR   DrugBank; DB03942; Carboxylic PRPP.
DR   DrugBank; DB01972; Guanosine-5'-Monophosphate.
DR   MEROPS; C44.001; -.
DR   jPOST; P0AG16; -.
DR   PaxDb; 511145-b2312; -.
DR   EnsemblBacteria; AAC75372; AAC75372; b2312.
DR   GeneID; 75172440; -.
DR   GeneID; 946794; -.
DR   KEGG; ecj:JW2309; -.
DR   KEGG; eco:b2312; -.
DR   PATRIC; fig|1411691.4.peg.4422; -.
DR   EchoBASE; EB0787; -.
DR   eggNOG; COG0034; Bacteria.
DR   InParanoid; P0AG16; -.
DR   OMA; IRHFGVK; -.
DR   OrthoDB; 9801213at2; -.
DR   PhylomeDB; P0AG16; -.
DR   BioCyc; EcoCyc:PRPPAMIDOTRANS-MONOMER; -.
DR   BioCyc; MetaCyc:PRPPAMIDOTRANS-MONOMER; -.
DR   BRENDA; 2.4.2.14; 2026.
DR   SABIO-RK; P0AG16; -.
DR   UniPathway; UPA00074; UER00124.
DR   EvolutionaryTrace; P0AG16; -.
DR   PHI-base; PHI:8488; -.
DR   PRO; PR:P0AG16; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0016757; F:glycosyltransferase activity; IDA:EcoliWiki.
DR   GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR   GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IDA:EcoliWiki.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   GO; GO:0006164; P:purine nucleotide biosynthetic process; IDA:EcoliWiki.
DR   CDD; cd00715; GPATase_N; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   DisProt; DP00578; -.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   HAMAP; MF_01931; PurF; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005854; PurF.
DR   InterPro; IPR035584; PurF_N.
DR   NCBIfam; TIGR01134; purF; 1.
DR   PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Glutamine amidotransferase;
KW   Glycosyltransferase; Magnesium; Metal-binding; Purine biosynthesis;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7037784"
FT   CHAIN           2..505
FT                   /note="Amidophosphoribosyltransferase"
FT                   /id="PRO_0000139638"
FT   DOMAIN          2..236
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   ACT_SITE        2
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931,
FT                   ECO:0000269|PubMed:7037784"
FT   BINDING         305
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   BINDING         367
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   BINDING         368
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   CONFLICT        45..46
FT                   /note="LR -> SL (in Ref. 2; AAA24453 and 3;
FT                   CAA23613/AAA24452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="G -> A (in Ref. 2; AAA24453 and 3;
FT                   CAA23613/AAA24452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        213..230
FT                   /note="ALDTLGFDFLRDVAPGEA -> GSIRWALISCVTSRRAR (in Ref. 2;
FT                   AAA24453 and 3; CAA23613/AAA24452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="V -> A (in Ref. 2; AAA24453 and 3;
FT                   CAA23613/AAA24452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        283
FT                   /note="L -> V (in Ref. 2; AAA24453 and 3;
FT                   CAA23613/AAA24452)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        337
FT                   /note="M -> I (in Ref. 2; AAA24453)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="A -> R (in Ref. 1; CAA30971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494
FT                   /note="N -> S (in Ref. 2; AAA24453 and 3;
FT                   CAA23613/AAA24452)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..8
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           14..23
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          30..37
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          43..50
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           58..63
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          66..74
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          78..80
FT                   /evidence="ECO:0007829|PDB:1ECJ"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:1ECC"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          97..105
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           108..119
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           128..140
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           150..163
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          166..174
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   TURN            175..177
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          178..183
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          192..197
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          203..210
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           211..216
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          220..224
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          229..237
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          239..243
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           254..258
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           272..290
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   TURN            291..293
FT                   /evidence="ECO:0007829|PDB:1ECF"
FT   STRAND          298..301
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   TURN            303..306
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           307..317
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          325..327
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          338..340
FT                   /evidence="ECO:0007829|PDB:1ECF"
FT   HELIX           346..350
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          351..353
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           355..357
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   TURN            358..360
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          363..368
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          371..373
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           374..385
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          389..397
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          406..408
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           413..415
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   TURN            417..420
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           423..430
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   STRAND          433..437
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           440..448
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           460..463
FT                   /evidence="ECO:0007829|PDB:6CZF"
FT   HELIX           473..498
FT                   /evidence="ECO:0007829|PDB:6CZF"
SQ   SEQUENCE   505 AA;  56488 MW;  50FD08EA85E6F2A8 CRC64;
     MCGIVGIAGV MPVNQSIYDA LTVLQHRGQD AAGIITIDAN NCFRLRKANG LVSDVFEARH
     MQRLQGNMGI GHVRYPTAGS SSASEAQPFY VNSPYGITLA HNGNLTNAHE LRKKLFEEKR
     RHINTTSDSE ILLNIFASEL DNFRHYPLEA DNIFAAIAAT NRLIRGAYAC VAMIIGHGMV
     AFRDPNGIRP LVLGKRDIDE NRTEYMVASE SVALDTLGFD FLRDVAPGEA IYITEEGQLF
     TRQCADNPVS NPCLFEYVYF ARPDSFIDKI SVYSARVNMG TKLGEKIARE WEDLDIDVVI
     PIPETSCDIA LEIARILGKP YRQGFVKNRY VGRTFIMPGQ QLRRKSVRRK LNANRAEFRD
     KNVLLVDDSI VRGTTSEQII EMAREAGAKK VYLASAAPEI RFPNVYGIDM PSATELIAHG
     REVDEIRQII GADGLIFQDL NDLIDAVRAE NPDIQQFECS VFNGVYVTKD VDQGYLDFLD
     TLRNDDAKAV QRQNEVENLE MHNEG
//