ID A0A271IV73_9BACT Unreviewed; 209 AA.
AC A0A271IV73;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=B1759_18750 {ECO:0000313|EMBL:PAP74459.1};
OS Rubrivirga sp. SAORIC476.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC Rubrivirga.
OX NCBI_TaxID=1961794 {ECO:0000313|EMBL:PAP74459.1, ECO:0000313|Proteomes:UP000216627};
RN [1] {ECO:0000313|EMBL:PAP74459.1, ECO:0000313|Proteomes:UP000216627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAORIC476 {ECO:0000313|EMBL:PAP74459.1,
RC ECO:0000313|Proteomes:UP000216627};
RA Kumagai Y., Kogure K., Yoshizawa S.;
RT "Whole genome sequence of Rhodothermus Rubrivirga sp. SAORIC476.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00036742,
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01930}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PAP74459.1}.
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; MVOI01000015; PAP74459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A271IV73; -.
DR OrthoDB; 9806170at2; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000216627; Unassembled WGS sequence.
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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01930}.
FT DOMAIN 1..184
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 11..13
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 104
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT SITE 147
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
SQ SEQUENCE 209 AA; 21941 MW; 4B10449851BFB8CD CRC64;
MRLAFFASGG GSNVGAILDA IDAGALRAEP VLLISDRPGC GALARAEARG LPTEVIAPLS
DETHFSDALL DALARAEADT VALAGYLRKI PAPVVWAFRD RILNVHPSLL PAFGGTGWYG
RRVHQGVLDA GCRVSGATVH LVDDQYDTGP IVLQEAVRVQ PDDTAETLAA RVLAVEHRLF
PDALALLADG RLRVADGRVS LLSTPPSAP
//
