ID   Q9CPL7_PASMU            Unreviewed;       213 AA.
AC   Q9CPL7;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   02-APR-2025, entry version 133.
DE   RecName: Full=Phosphoribosylglycinamide formyltransferase {ECO:0000256|HAMAP-Rule:MF_01930};
DE            EC=2.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01930};
DE   AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|HAMAP-Rule:MF_01930};
DE   AltName: Full=GAR transformylase {ECO:0000256|HAMAP-Rule:MF_01930};
DE            Short=GART {ECO:0000256|HAMAP-Rule:MF_01930};
GN   Name=purN {ECO:0000256|HAMAP-Rule:MF_01930,
GN   ECO:0000313|EMBL:AAK02104.1};
GN   OrderedLocusNames=PM0020 {ECO:0000313|EMBL:AAK02104.1};
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK02104.1, ECO:0000313|Proteomes:UP000000809};
RN   [1] {ECO:0000313|EMBL:AAK02104.1, ECO:0000313|Proteomes:UP000000809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70 {ECO:0000313|EMBL:AAK02104.1,
RC   ECO:0000313|Proteomes:UP000000809};
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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:0000256|HAMAP-Rule:MF_01930}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(1)-(5-phospho-beta-D-ribosyl)glycinamide + (6R)-10-
CC         formyltetrahydrofolate = N(2)-formyl-N(1)-(5-phospho-beta-D-
CC         ribosyl)glycinamide + (6S)-5,6,7,8-tetrahydrofolate + H(+);
CC         Xref=Rhea:RHEA:15053, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453,
CC         ChEBI:CHEBI:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366;
CC         EC=2.1.2.2; Evidence={ECO:0000256|ARBA:ARBA00047664,
CC         ECO:0000256|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:0000256|ARBA:ARBA00005054, ECO:0000256|HAMAP-Rule:MF_01930}.
CC   -!- SIMILARITY: Belongs to the GART family. {ECO:0000256|ARBA:ARBA00038440,
CC       ECO:0000256|HAMAP-Rule:MF_01930}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004439; AAK02104.1; -; Genomic_DNA.
DR   RefSeq; WP_005722268.1; NC_002663.1.
DR   AlphaFoldDB; Q9CPL7; -.
DR   STRING; 272843.PM0020; -.
DR   EnsemblBacteria; AAK02104; AAK02104; PM0020.
DR   KEGG; pmu:PM0020; -.
DR   PATRIC; fig|272843.6.peg.20; -.
DR   HOGENOM; CLU_038395_1_1_6; -.
DR   OrthoDB; 9806170at2; -.
DR   UniPathway; UPA00074; UER00126.
DR   Proteomes; UP000000809; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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   Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 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   InterPro; IPR001555; GART_AS.
DR   NCBIfam; TIGR00639; PurN; 1.
DR   PANTHER; PTHR43369; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   PANTHER; PTHR43369:SF2; PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   SUPFAM; SSF53328; Formyltransferase; 1.
DR   PROSITE; PS00373; GART; 1.
PE   3: Inferred from homology;
KW   Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW   Rule:MF_01930}; Reference proteome {ECO:0000313|Proteomes:UP000000809};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01930}.
FT   DOMAIN          2..182
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   ACT_SITE        109
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_01930"
FT   BINDING         66
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   BINDING         90..93
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   BINDING         107
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   SITE            145
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
SQ   SEQUENCE   213 AA;  23605 MW;  DFB46FB813ABB5BB CRC64;
     MKKIVVLVSG HGSNLQALID ACHSGQIAGK IVAVISNQAE AYALERAQSA SIPSKVFLRK
     DFANNRAMDE QIGHYIESVQ ADLIVLAGYM KILSPAFTQR FAGKILNIHP SLLPKYPGLN
     TYQQALDAGE REHGTSVHFV NEEVDAGAVI LQAKVPIFAE DRIEDIEQRV KAQELRIYPL
     VVKWFVEERL TLIGEHAFLD GKQLPPQGYA MEE
//