PUR3_STAAS
ID PUR3_STAAS Reviewed; 188 AA.
AC Q6GAE1;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000255|HAMAP-Rule:MF_01930};
DE EC=2.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01930};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000255|HAMAP-Rule:MF_01930};
DE AltName: Full=GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01930};
DE Short=GART {ECO:0000255|HAMAP-Rule:MF_01930};
GN Name=purN {ECO:0000255|HAMAP-Rule:MF_01930}; OrderedLocusNames=SAS1008;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC -!- FUNCTION: Catalyzes the transfer of a formyl group from 10-
CC formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR),
CC producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and
CC tetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01930}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-
CC ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-
CC formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide;
CC Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC ChEBI:CHEBI:57454, ChEBI:CHEBI:143788, ChEBI:CHEBI:147286;
CC EC=2.1.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01930};
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 (10-formyl THF route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01930}.
CC -!- SIMILARITY: Belongs to the GART family. {ECO:0000255|HAMAP-
CC Rule:MF_01930}.
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DR EMBL; BX571857; CAG42782.1; -; Genomic_DNA.
DR RefSeq; WP_000238663.1; NC_002953.3.
DR AlphaFoldDB; Q6GAE1; -.
DR SMR; Q6GAE1; -.
DR KEGG; sas:SAS1008; -.
DR HOGENOM; CLU_038395_1_3_9; -.
DR OMA; TGITIHY; -.
DR UniPathway; UPA00074; UER00126.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd08645; FMT_core_GART; 1.
DR HAMAP; MF_01930; PurN; 1.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR004607; GART.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR SUPFAM; SSF53328; SSF53328; 1.
DR TIGRFAMs; TIGR00639; PurN; 1.
PE 3: Inferred from homology;
KW Purine biosynthesis; Transferase.
FT CHAIN 1..188
FT /note="Phosphoribosylglycinamide formyltransferase"
FT /id="PRO_0000074949"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT BINDING 12..14
FT /ligand="N(1)-(5-phospho-beta-D-ribosyl)glycinamide"
FT /ligand_id="ChEBI:CHEBI:143788"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT BINDING 66
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT BINDING 91..94
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT BINDING 108
FT /ligand="(6S)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:57454"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
FT SITE 146
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01930"
SQ SEQUENCE 188 AA; 21153 MW; D034134258D89AEE CRC64;
MVKIAIFASG SGSNFENIVE HVESGKLENI EVTALYTDHQ NAFCIDRAKK HDIPVYINEP
KQFDSKAAYE QHLVSLLNED KVEWIILAGY MRLIGPDLLA SFEGKILNIH PSLLPKYKGI
DAIGQAYHSG DTITGSTVHY VDCGMDTGEI IEQRQCDIRP DDSKEQLEEK VKKLEYELYP
SVIAKIVK