ID W5XZ31_9CORY Unreviewed; 172 AA.
AC W5XZ31;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=phosphoribosylglycinamide formyltransferase 1 {ECO:0000256|ARBA:ARBA00012254};
DE EC=2.1.2.2 {ECO:0000256|ARBA:ARBA00012254};
DE AltName: Full=5'-phosphoribosylglycinamide transformylase {ECO:0000256|ARBA:ARBA00041682};
DE AltName: Full=GAR transformylase {ECO:0000256|ARBA:ARBA00041324};
GN Name=purN {ECO:0000313|EMBL:AHI22276.1};
GN ORFNames=B843_04435 {ECO:0000313|EMBL:AHI22276.1};
OS Corynebacterium vitaeruminis DSM 20294.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI22276.1, ECO:0000313|Proteomes:UP000019222};
RN [1] {ECO:0000313|EMBL:AHI22276.1, ECO:0000313|Proteomes:UP000019222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium vitaeruminis DSM 20294.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the GART family.
CC {ECO:0000256|ARBA:ARBA00038440}.
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DR EMBL; CP004353; AHI22276.1; -; Genomic_DNA.
DR AlphaFoldDB; W5XZ31; -.
DR STRING; 1224164.B843_04435; -.
DR KEGG; cvt:B843_04435; -.
DR PATRIC; fig|1224164.3.peg.880; -.
DR eggNOG; COG0299; Bacteria.
DR HOGENOM; CLU_038395_1_0_11; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000019222; Chromosome.
DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd08645; FMT_core_GART; 1.
DR Gene3D; 3.40.50.170; Formyl transferase, N-terminal domain; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019222};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AHI22276.1}.
FT DOMAIN 2..151
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
SQ SEQUENCE 172 AA; 18498 MW; 7C90DC994E1DCC98 CRC64;
MIGVVTDVDC PAIERARKAG IPAVTVPLEK GADREVWNEQ LAEAVGSFDP HLVVSAGFMK
ILGSTFLERF GGRIINTHPA LLPSFPGAHA VRDALAYGVK VTGSTVHFVD EGVDTGKIIA
QKPVEIMPGE REEDLHERIK QVERKLIVSV LNSAVVVMGA EKNSGEVSFT NE
//