FTHS_BACFR
ID FTHS_BACFR Reviewed; 555 AA.
AC Q64U80;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BF2202;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(2004).
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; AP006841; BAD48949.1; -; Genomic_DNA.
DR RefSeq; WP_005787533.1; NC_006347.1.
DR RefSeq; YP_099483.1; NC_006347.1.
DR AlphaFoldDB; Q64U80; -.
DR SMR; Q64U80; -.
DR STRING; 295405.BF2202; -.
DR EnsemblBacteria; BAD48949; BAD48949; BF2202.
DR GeneID; 66328797; -.
DR KEGG; bfr:BF2202; -.
DR PATRIC; fig|295405.11.peg.2140; -.
DR HOGENOM; CLU_003601_3_3_10; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002197; 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.
FT CHAIN 1..555
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199333"
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
