ID Q83GZ2_TROWT Unreviewed; 215 AA.
AC Q83GZ2;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 104.
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:AAO44180.1};
GN OrderedLocusNames=TWT_083 {ECO:0000313|EMBL:AAO44180.1};
OS Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Tropherymataceae;
OC Tropheryma.
OX NCBI_TaxID=203267 {ECO:0000313|EMBL:AAO44180.1, ECO:0000313|Proteomes:UP000002200};
RN [1] {ECO:0000313|EMBL:AAO44180.1, ECO:0000313|Proteomes:UP000002200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Twist {ECO:0000313|EMBL:AAO44180.1,
RC ECO:0000313|Proteomes:UP000002200};
RX PubMed=12902375; DOI=10.1101/gr.1474603;
RA Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA Claverie J.-M.;
RT "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT reduced genome.";
RL Genome Res. 13:1800-1809(2003).
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=(6R)-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:143788, ChEBI:CHEBI:147286, ChEBI:CHEBI:195366;
CC EC=2.1.2.2; Evidence={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|HAMAP-
CC Rule:MF_01930}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01930}.
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DR EMBL; AE014184; AAO44180.1; -; Genomic_DNA.
DR AlphaFoldDB; Q83GZ2; -.
DR STRING; 203267.TWT_083; -.
DR KEGG; twh:TWT_083; -.
DR eggNOG; COG0299; Bacteria.
DR HOGENOM; CLU_038395_1_0_11; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000002200; 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 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 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.
PE 3: Inferred from homology;
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755, ECO:0000256|HAMAP-
KW Rule:MF_01930}; Reference proteome {ECO:0000313|Proteomes:UP000002200};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01930}.
FT DOMAIN 8..187
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 70
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 95..98
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 112
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT SITE 150
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
SQ SEQUENCE 215 AA; 23637 MW; 007B11F7946334B2 CRC64;
MSDMKTAMRL IVMVSGIGSG LLRLIRACEQ KELKAEIVAV GSDRHAPALS HASDYGIPFF
VSPFKEYSNR DAWGANLLNT VLAYKPDLVV LSGFMRILPS CVVDALSPNL INTHPSYLPE
FPGMNAVEDA LRAGVKTTGA SVIRVDNGID TGPVISQMRV KVYSSDTCQT LHSRIKKVEH
LLLCRAIKNI YTEQFILKNL LHNSVRRPSG KTGDR
//
