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Database: UniProt
Entry: P39771
LinkDB: P39771
Original site: P39771 
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   05-DEC-2018, entry version 133.
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};
GN   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
RT   formate-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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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
CC       of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP
CC       and beta GAR; the second, a side reaction, is the production of
CC       acetyl phosphate and ADP from acetate and ATP.
CC   -!- FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes
CC       the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR),
CC       producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is
CC       provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate.
CC       {ECO:0000255|HAMAP-Rule:MF_01643}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + formate + N(1)-(5-phospho-D-ribosyl)glycinamide =
CC         ADP + H(+) + N(2)-formyl-N(1)-(5-phospho-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:58426, ChEBI:CHEBI:58457, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01643};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC       N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-
CC       phospho-D-ribosyl)glycinamide (formate route): step 1/1.
CC       {ECO:0000255|HAMAP-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   ProteinModelPortal; P39771; -.
DR   SMR; P39771; -.
DR   STRING; 224308.Bsubs1_010100001238; -.
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;
KW   ATP-binding; Complete proteome; Magnesium; Metal-binding;
KW   Nucleotide-binding; Purine biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN         1    384       Formate-dependent
FT                                phosphoribosylglycinamide
FT                                formyltransferase.
FT                                /FTId=PRO_0000074955.
FT   DOMAIN      111    300       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   NP_BIND     152    157       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   NP_BIND     187    190       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION       14     15       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   REGION      355    356       5'-phosphoribosylglycinamide binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   METAL       259    259       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   METAL       271    271       Magnesium. {ECO:0000255|HAMAP-
FT                                Rule:MF_01643}.
FT   BINDING      74     74       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     106    106       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     147    147       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     195    195       ATP. {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     278    278       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   BINDING     348    348       5'-phosphoribosylglycinamide.
FT                                {ECO:0000255|HAMAP-Rule:MF_01643}.
FT   CONFLICT    240    241       KH -> ND (in Ref. 1; CAA55557).
FT                                {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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