FTHS_BACFN
ID FTHS_BACFN Reviewed; 555 AA.
AC Q5LD60;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Formate--tetrahydrofolate ligase {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=BF2256;
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-
CC formyltetrahydrofolate + ADP + phosphate; Xref=Rhea:RHEA:20221,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57453, ChEBI:CHEBI:57454, ChEBI:CHEBI:456216; EC=6.3.4.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01543};
CC -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC {ECO:0000255|HAMAP-Rule:MF_01543}.
CC -!- SIMILARITY: Belongs to the formate--tetrahydrofolate ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_01543}.
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DR EMBL; CR626927; CAH07950.1; -; Genomic_DNA.
DR RefSeq; WP_005787533.1; NC_003228.3.
DR AlphaFoldDB; Q5LD60; -.
DR SMR; Q5LD60; -.
DR STRING; 272559.BF9343_2169; -.
DR EnsemblBacteria; CAH07950; CAH07950; BF9343_2169.
DR GeneID; 66328797; -.
DR KEGG; bfs:BF9343_2169; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_10; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006731; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035999; P:tetrahydrofolate interconversion; IEA:UniProtKB-UniPathway.
DR CDD; cd00477; FTHFS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01543; FTHFS; 1.
DR InterPro; IPR000559; Formate_THF_ligase.
DR InterPro; IPR020628; Formate_THF_ligase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01268; FTHFS; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00721; FTHFS_1; 1.
DR PROSITE; PS00722; FTHFS_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..555
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199334"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 555 AA; 60418 MW; E5497181B20F7530 CRC64;
MKSDIEIARS VELKKIKQVA ESIGIPRDEV ENYGRYIAKI PEYLIDEEKV KKSNLILVTA
ITATKAGIGK TTVSIGLALG LNKIGKKAIV ALREPSLGPC FGMKGGAAGG GYAQVLPMEK
INLHFTGDFH AITSAHNMIS ALLDNYLYQN QSKGFGLKEI LWRRVLDVND RSLRNIVVGL
GPKTNGITQE SGFDITPASE IMAILCLSKD VDDLRRRIEN ILLGYTYDNK PFTVKDLGVA
GAITVLLKDA IHPNLVQTTE GTAAFVHGGP FANIAHGCNS ILATKMAMTF GDYVITEAGF
GADLGAEKFY NIKCRKSGLQ PRLTVIVATA QGLKMHGGVS LDRIKEPNLE GLREGLRNLD
KHVRNLHSFG QTVIVAFNKF ASDTDEEMEL LREHCEQLGV GYAINNAFSE GGEGAVDLAN
LVVETIENKP SEPLQFTYND EDSVQQKIEK VATNLYGASV VTYSTLTRNK IKLIEEMGIG
HYPVCIAKTQ YSFSADPKVY GAVDNFELHI KDIVINNGAE MIVAIAGEIM RMPGLPKEPQ
ALHIDIVDGN IEGLS