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Database: UniProt
Entry: S2KT83_HALAF
LinkDB: S2KT83_HALAF
Original site: S2KT83_HALAF 
ID   S2KT83_HALAF            Unreviewed;       248 AA.
AC   S2KT83;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=L861_04685 {ECO:0000313|EMBL:EPC03728.1};
OS   Halomonas anticariensis (strain DSM 16096 / CECT 5854 / LMG 22089 / FP35).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1121939 {ECO:0000313|EMBL:EPC03728.1, ECO:0000313|Proteomes:UP000014463};
RN   [1] {ECO:0000313|EMBL:EPC03728.1, ECO:0000313|Proteomes:UP000014463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16096 / CECT 5854 / LMG 22089 / FP35
RC   {ECO:0000313|Proteomes:UP000014463};
RX   PubMed=23868129; DOI=10.1128/genomeA.00497-13;
RA   Tahrioui A., Quesada E., Llamas I.;
RT   "Draft genome sequence of the moderately halophilic gammaproteobacterium
RT   Halomonas anticariensis FP35.";
RL   Genome Announc. 1:31-31(2013).
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:EPC03728.1}.
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DR   EMBL; ASTJ01000011; EPC03728.1; -; Genomic_DNA.
DR   RefSeq; WP_016415365.1; NZ_KE332377.1.
DR   AlphaFoldDB; S2KT83; -.
DR   STRING; 1121939.L861_04685; -.
DR   PATRIC; fig|1121939.11.peg.884; -.
DR   eggNOG; COG0299; Bacteria.
DR   OMA; TGITIHY; -.
DR   OrthoDB; 9806170at2; -.
DR   UniPathway; UPA00074; UER00126.
DR   Proteomes; UP000014463; 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   PIRSF; PIRSF036480; FormyFH4_hydr; 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:UP000014463};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01930}.
FT   DOMAIN          23..201
FT                   /note="Formyl transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00551"
FT   REGION          223..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   BINDING         32..34
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         85
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   BINDING         110..113
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   BINDING         127
FT                   /ligand="(6R)-10-formyltetrahydrofolate"
FT                   /ligand_id="ChEBI:CHEBI:195366"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
FT   SITE            165
FT                   /note="Raises pKa of active site His"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01930"
SQ   SEQUENCE   248 AA;  27168 MW;  1715F9BBC4508EBD CRC64;
     MSNDQYSSDT LTDFTPETTE PRRVVVLISG NGSNLQALID AQSHGELGGE IVAVISNQPN
     AYGLKRARDA GIDAVVLPHR EYESREAFDG ALIKVIERHE PDLIVLAGFM RILSPIFVQR
     FYGRLLNIHP SLLPAYQGLD THARVLADGA KEHGASVHFV TEELDGGPVV IQAALEITED
     DSVETLKNKV HSREHLIYPI AVKWFLEGRL RLGAEGATFD GVPLPPQGMR MSHADAAEEL
     DEDIGEES
//
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