(data stored in ACNUC7421 zone)

SWISSPROT: PURT_BACSU

ID   PURT_BACSU              Reviewed;         384 AA.
AC   P39771; O31450;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   11-DEC-2019, entry version 136.
DE   RecName: Full=Formate-dependent phosphoribosylglycinamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Formate-dependent GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01643};
DE            EC=2.1.2.- {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=GAR transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE            Short=GART 2 {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Non-folate glycinamide ribonucleotide transformylase {ECO:0000255|HAMAP-Rule:MF_01643};
DE   AltName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01643};
GN   Name=purT {ECO:0000255|HAMAP-Rule:MF_01643}; OrderedLocusNames=BSU02230;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7496533; DOI=10.1099/13500872-141-9-2211;
RA   Saxild H.H., Jacobsen J.H., Nygaard P.;
RT   "Functional analysis of the Bacillus subtilis purT gene encoding formate-
RT   dependent glycinamide ribonucleotide transformylase.";
RL   Microbiology 141:2211-2218(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RA   Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT   "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT   Bacillus subtilis chromosome.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
CC   -!- FUNCTION: Catalyzes two reactions: the first one is the production of
CC       beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP and beta
CC       GAR; the second, a side reaction, is the production of acetyl phosphate
CC       and ADP from acetate and ATP.
CC   -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the
CC       transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing
CC       5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by
CC       PurU via hydrolysis of 10-formyl-tetrahydrofolate. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + formate + N(1)-(5-phospho-D-ribosyl)glycinamide = ADP +
CC         H(+) + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + phosphate;
CC         Xref=Rhea:RHEA:24829, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58426,
CC         ChEBI:CHEBI:58457, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01643};
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}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP-
CC       Rule:MF_01643}.
DR   EMBL; X78962; CAA55557.1; -; Genomic_DNA.
DR   EMBL; AB006424; BAA33120.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12017.1; -; Genomic_DNA.
DR   PIR; E69685; E69685.
DR   RefSeq; NP_388105.1; NC_000964.3.
DR   RefSeq; WP_003246432.1; NZ_JNCM01000030.1.
DR   SMR; P39771; -.
DR   STRING; 224308.BSU02230; -.
DR   PaxDb; P39771; -.
DR   PRIDE; P39771; -.
DR   EnsemblBacteria; CAB12017; CAB12017; BSU02230.
DR   GeneID; 938438; -.
DR   KEGG; bsu:BSU02230; -.
DR   PATRIC; fig|224308.179.peg.229; -.
DR   eggNOG; ENOG4108HH9; Bacteria.
DR   eggNOG; COG0027; LUCA.
DR   HOGENOM; HOG000072820; -.
DR   InParanoid; P39771; -.
DR   KO; K08289; -.
DR   OMA; GMVTMIT; -.
DR   PhylomeDB; P39771; -.
DR   BioCyc; BSUB:BSU02230-MONOMER; -.
DR   UniPathway; UPA00074; UER00127.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; 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   3: Inferred from homology;
DR   PRODOM; P39771.
DR   SWISS-2DPAGE; P39771.
KW   ATP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Purine biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..384
FT                   /note="Formate-dependent phosphoribosylglycinamide
FT                   formyltransferase"
FT                   /id="PRO_0000074955"
FT   DOMAIN          111..300
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   NP_BIND         152..157
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   NP_BIND         187..190
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   REGION          14..15
FT                   /note="5'-phosphoribosylglycinamide binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   REGION          355..356
FT                   /note="5'-phosphoribosylglycinamide binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   METAL           259
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   METAL           271
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         74
FT                   /note="5'-phosphoribosylglycinamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         106
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         147
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         195
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         278
FT                   /note="5'-phosphoribosylglycinamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   BINDING         348
FT                   /note="5'-phosphoribosylglycinamide"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01643"
FT   CONFLICT        240..241
FT                   /note="KH -> ND (in Ref. 1; CAA55557)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   384 AA;  42093 MW;  5E3642CD6CAF90F7 CRC64;
     MYQSKKVLLL GSGELGKEVV IEAQRLGVQT VAVDSYEHAP AMQVAHNSYV VDMLDPEQIR
     TIIEKENPDL IVPEVEAIAT DELLKLEEEG FHVIPNARAA KLTMDREGIR RLAAETLGLA
     TAGYEFANTY DEFIQAAAQI GFPCVVKPLM SSSGKGQSVC RSEADLESCW ETAMEGGRVK
     NGRVIVEEFI PFESEITLLT VRAVNGTAFC EPIGHVQKDG DYIESWQPHD MTEQQIEEAK
     HIAKTITDEL GGYGLFGVEL FLAKDRVYFS EVSPRPHDTG LVTLVTQNLS EFALHVRAIL
     GFPITEITQL SPGASRPLKA PEELADYTVE GLENALAVPK TQVRVFGKPI TKAGRRMAVA
     LSAADSVETA RENAKKALDQ LILK
//

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