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Database: UniProt
Entry: A0A0P0DC66_9FLAO
LinkDB: A0A0P0DC66_9FLAO
Original site: A0A0P0DC66_9FLAO 
ID   A0A0P0DC66_9FLAO        Unreviewed;       187 AA.
AC   A0A0P0DC66;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=APS56_11410 {ECO:0000313|EMBL:ALJ05695.1};
OS   Pseudalgibacter alginicilyticus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Pseudalgibacter.
OX   NCBI_TaxID=1736674 {ECO:0000313|EMBL:ALJ05695.1, ECO:0000313|Proteomes:UP000057981};
RN   [1] {ECO:0000313|EMBL:ALJ05695.1, ECO:0000313|Proteomes:UP000057981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HZ-22 {ECO:0000313|Proteomes:UP000057981};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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; CP012898; ALJ05695.1; -; Genomic_DNA.
DR   RefSeq; WP_054728205.1; NZ_CP012898.1.
DR   AlphaFoldDB; A0A0P0DC66; -.
DR   STRING; 1736674.APS56_11410; -.
DR   KEGG; ahz:APS56_11410; -.
DR   PATRIC; fig|1736674.3.peg.2339; -.
DR   OrthoDB; 9806170at2; -.
DR   UniPathway; UPA00074; UER00126.
DR   Proteomes; UP000057981; 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   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:UP000057981};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ALJ05695.1}.
FT   DOMAIN          2..182
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
SQ   SEQUENCE   187 AA;  20907 MW;  75DE7C6E572BD198 CRC64;
     MKRIVIFASG SGSNAENLIK FFHNRKNASV IQVLTNNPHA KVIDRCNKLQ VSCLSFNKIA
     LNKTNDVLNI LNASNPDLIV LAGFLWKFPE TILNAYPNKV INVHPALLPK FGGKGMYGMH
     VHEAVVSNKE TETGITIHYV NENYDEGATI FQAKCKVLVT DTAEDVAKKI HLLEMEHFPK
     VVQRLLK
//
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