ID W7QGT8_9ALTE Unreviewed; 216 AA.
AC W7QGT8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=DS2_00485 {ECO:0000313|EMBL:EWH12154.1};
OS Catenovulum agarivorans DS-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Catenovulum.
OX NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH12154.1, ECO:0000313|Proteomes:UP000019276};
RN [1] {ECO:0000313|EMBL:EWH12154.1, ECO:0000313|Proteomes:UP000019276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-2 {ECO:0000313|EMBL:EWH12154.1,
RC ECO:0000313|Proteomes:UP000019276};
RX PubMed=24604650;
RA Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL Genome Announc. 2:e00144-14(2014).
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: 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:EWH12154.1}.
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DR EMBL; ARZY01000001; EWH12154.1; -; Genomic_DNA.
DR RefSeq; WP_035012615.1; NZ_ARZY01000001.1.
DR AlphaFoldDB; W7QGT8; -.
DR STRING; 1328313.DS2_00485; -.
DR PATRIC; fig|1328313.3.peg.105; -.
DR eggNOG; COG0299; Bacteria.
DR OrthoDB; 9806170at2; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000019276; 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}; Reference proteome {ECO:0000313|Proteomes:UP000019276};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01930}.
FT DOMAIN 3..183
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT ACT_SITE 110
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 13..15
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 91..94
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 108
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT SITE 146
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
SQ SEQUENCE 216 AA; 23586 MW; 0945B1217CC2FC3C CRC64;
MSKNIVVLIS GSGSNLQAII DACQSGQIDG RISAVVSNKA DAYGLVRAEN ASIPTHTLNH
KSFASREDYD TELAKLIDSY QPDLVVLAGF MRILTAGFVQ KFVGKMLNIH PSLLPKYQGL
NTHQRALDAG DKEHGVSVHF VTEELDGGPV VCQASIDVAQ TDTADSLAQR IHVKEHIIYP
LVVDWFCKGK LTMKNGQAWL DNKVLPATGI RYVEEN
//
