ID A0A1X7RY83_ZYMTR Unreviewed; 219 AA.
AC A0A1X7RY83;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ORFNames=ZT3D7_G7304 {ECO:0000313|EMBL:SMQ52151.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ52151.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ52151.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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; LT853698; SMQ52151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7RY83; -.
DR STRING; 1276538.A0A1X7RY83; -.
DR UniPathway; UPA00074; UER00126.
DR Proteomes; UP000215127; Chromosome 7.
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 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:UP000215127};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..204
FT /note="Formyl transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00551"
SQ SEQUENCE 219 AA; 23875 MW; 8176262AEC0F2C1D CRC64;
MAPPTRITVL ISGSGTNLQA LIDASKTSSL SNTTFVRVIS DRKSAYGLIR ASNANIPTSY
HSILPYKKSH PDTSSNPTFN AAREAYDADL AKLVLADEPQ LVVCAGFMRI LTPSFLNPLA
MANVPIINLH PSLHGDLIGA GCIERAWEEF QQGRRKKTGI MIHYVIAEVD MGEPILQKEV
DIEGCTSLVD LQARIHEAEH VLIVDGASTV VEKIRTTRD
//
