ID   PUR3_STAAM              Reviewed;         188 AA.
AC   P65897; Q99V25;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=SAV1072;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
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; BA000017; BAB57234.1; -; Genomic_DNA.
DR   RefSeq; WP_000238669.1; NC_002758.2.
DR   AlphaFoldDB; P65897; -.
DR   SMR; P65897; -.
DR   World-2DPAGE; 0002:P65897; -.
DR   PaxDb; P65897; -.
DR   EnsemblBacteria; BAB57234; BAB57234; SAV1072.
DR   KEGG; sav:SAV1072; -.
DR   HOGENOM; CLU_038395_1_3_9; -.
DR   OMA; TGITIHY; -.
DR   PhylomeDB; P65897; -.
DR   BioCyc; SAUR158878:SAV_RS05780-MON; -.
DR   UniPathway; UPA00074; UER00126.
DR   Proteomes; UP000002481; Chromosome.
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_0000074946"
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;  21166 MW;  F0364618F275FA30 CRC64;
     MVKIAIFASG SGSNFENIVE HVESGKLENI EVTALYTDHQ NAFCIDRAKK HDIPVYINEP
     KQFDSKAAYE QHLVTLLNKD KVEWIILAGY MRLIGPDLLA SFEGKILNIH PSLLPKYKGI
     DAIGQAYHSG DTITGSTVHY VDCGMDTGEI IEQRQCDIRP DDSKEQLEEK VKKLEYELYP
     SVIAKIVK