ID W7E769_9PROT Unreviewed; 205 AA.
AC W7E769;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=COMX_04580 {ECO:0000313|EMBL:EUK18996.1};
OS Commensalibacter papalotli (ex Servin-Garciduenas et al. 2014).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=1208583 {ECO:0000313|EMBL:EUK18996.1, ECO:0000313|Proteomes:UP000019250};
RN [1] {ECO:0000313|EMBL:EUK18996.1, ECO:0000313|Proteomes:UP000019250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX-MONARCH01 {ECO:0000313|Proteomes:UP000019250};
RX PubMed=24604647;
RA Servin-Garciduenas L.E., Sanchez-Quinto A., Martinez-Romero E.;
RT "Draft Genome Sequence of Commensalibacter papalotli MX01, a Symbiont
RT Identified from the Guts of Overwintering Monarch Butterflies.";
RL Genome Announc. 2:e00128-14(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|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: 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:EUK18996.1}.
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DR EMBL; ATSX01000001; EUK18996.1; -; Genomic_DNA.
DR RefSeq; WP_034337557.1; NZ_ATSX01000001.1.
DR AlphaFoldDB; W7E769; -.
DR STRING; 1208583.COMX_04580; -.
DR PATRIC; fig|1208583.4.peg.926; -.
DR eggNOG; COG0299; Bacteria.
DR OrthoDB; 9806170at2; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000019250; 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 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:UP000019250};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01930}.
FT DOMAIN 6..186
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
FT ACT_SITE 113
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 15..17
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 69
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 94..97
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT BINDING 111
FT /ligand="(6R)-10-formyltetrahydrofolate"
FT /ligand_id="ChEBI:CHEBI:195366"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT SITE 149
FT /note="Raises pKa of active site His"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
SQ SEQUENCE 205 AA; 22378 MW; 300E0BB91AF09517 CRC64;
MTFKERIAIL ISGRGSNMDA LIEACKKPSF PASIKLVISN NPDAAGLDAA REAGIPTQVI
DHHGFGKDRQ AHERQIDAAL QAHNISVVCL AGYMRILTPF LINNWEGKIL NIHPSILPLF
PGLDTHAKAI KAGMKVHGCT VHIVTEVMDE GPILGQAIVP ILPDDTEHSL AKRLLKQEHL
LYSQVLKNFI HKEEPEASVD ALING
//