FTHS_CLOPE
ID FTHS_CLOPE Reviewed; 556 AA.
AC Q8XHL4;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=CPE2469;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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; BA000016; BAB82175.1; -; Genomic_DNA.
DR RefSeq; WP_003459368.1; NC_003366.1.
DR AlphaFoldDB; Q8XHL4; -.
DR SMR; Q8XHL4; -.
DR STRING; 195102.gene:10491796; -.
DR EnsemblBacteria; BAB82175; BAB82175; BAB82175.
DR KEGG; cpe:CPE2469; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000818; 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..556
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199340"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 556 AA; 60253 MW; 19AB7A9D7151A7C6 CRC64;
MKNDIEIAQS AKMEPIINIA KKIGLGEDDI ELYGKYKCKI SLDAIKKLEN NKDGKLVLVT
AINPTPAGEG KSTVTVGLGQ ALNKIGKNTV IALREPSLGP VFGIKGGAAG GGYAQVVPME
DINLHFTGDM HAITSANNLL CAAIDNHIHQ GNLLRIDSRR IVFKRVMDMN DRALRNIVVG
MGGKINGFLR EDGFMITVAS EIMAILCMAS DLEDLKERMG NILIAYNLDG EPVYAKELEV
QGAMALLMKD AIKPNLVQTL ENTPAIIHGG PFANIAHGCN SIIATKTALK MSDITITEAG
FGADLGAEKF LDIKCRYGNL NPDCVVLVAT IRALKHHGGV KKDELNISNV DALNKGMKNL
EKQIENIKAY GVPVVVAINK FITDSDEEVK AIEDFCKNIG VEVSLTEVWE KGGEGGIDLA
NKVIKTMETE PSNFKMIYDS EESIKDKILK IVQTIYGGKG VNYTPQALKQ IAEIEKFNLD
KLPICMAKTQ YSLSDNPSLL GRPENFDITV KEVRVSNGAG FIVVLTGDVM TMPGLPKVPA
ANRMDIKDNG EIVGLF
