PUR3_STAAW
ID PUR3_STAAW Reviewed; 188 AA.
AC Q8NX89;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, 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=MW0955;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(2002).
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; BA000033; BAB94820.1; -; Genomic_DNA.
DR RefSeq; WP_000238663.1; NC_003923.1.
DR AlphaFoldDB; Q8NX89; -.
DR SMR; Q8NX89; -.
DR EnsemblBacteria; BAB94820; BAB94820; BAB94820.
DR KEGG; sam:MW0955; -.
DR HOGENOM; CLU_038395_1_3_9; -.
DR OMA; TGITIHY; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000000418; 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_0000074950"
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