FTHS_CORDI
ID FTHS_CORDI Reviewed; 550 AA.
AC Q6NH87;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=DIP1253;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(2003).
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; BX248357; CAE49782.1; -; Genomic_DNA.
DR RefSeq; WP_010934929.1; NC_002935.2.
DR AlphaFoldDB; Q6NH87; -.
DR SMR; Q6NH87; -.
DR STRING; 257309.DIP1253; -.
DR PRIDE; Q6NH87; -.
DR EnsemblBacteria; CAE49782; CAE49782; DIP1253.
DR KEGG; cdi:DIP1253; -.
DR HOGENOM; CLU_003601_3_3_11; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002198; 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..550
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199342"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 550 AA; 58098 MW; 27D7F2392BABA05D CRC64;
MPTDVEIAQA HTLEPITDIA NRAGVPSDAL IPYGFTKAKI DINRIASENT GKLVLVTGIS
PTPAGEGKST VLIGLSDAMR LRGHNSIVAI REPSLGPVMG IKGGAAGGGY SQIVPMEDIN
LHFTGDFHAI TAANNTLAAM IDNHIHQGNT LGIDVRRITW QRCLDVNDRC LRKVVTGLGG
KAHGVPTETG FTITAASEIM AILCLALDLT DLEARLARIV VGQTFSSEPV TVGQLNAQGA
LAALLRDAVN PNLVQTLGGT PALCHGGPFA NIAHGCNSLI ATKTALSLGD VVLTEAGFGS
DLGAEKFFDI KSRVGDLNVA ATVVVATVRS LKYNAGVPKD ELTTENLEAL ASGVVNLERH
VENIRAFGIE PIVALNKFAS DTDAEINQLK AWAETMSVQL IPVEVWAHGG QGALELADAV
AVSMQNQTSH HLYDPELGIE ASLLTIAQKI YGAADVELSK QARQDLAYLQ ENGWDRLPVC
ISKTQYSFSD DPSQLGRPEG HTLHVRNLLP RIGAGFIVAL TGDVMTMPGL PKKPAAENIG
VENGEIKGLF