FTHS_CAMC5
ID FTHS_CAMC5 Reviewed; 550 AA.
AC A7GZZ0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Ccur92_14780;
GN ORFNames=CCV52592_0358;
OS Campylobacter curvus (strain 525.92).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360105;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=525.92;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Genome sequence of Campylobacter curvus 525.92 isolated from human
RT feces.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000767; EAT99584.1; -; Genomic_DNA.
DR RefSeq; WP_011992625.1; NC_009715.2.
DR AlphaFoldDB; A7GZZ0; -.
DR SMR; A7GZZ0; -.
DR STRING; 360105.CCV52592_0358; -.
DR EnsemblBacteria; EAT99584; EAT99584; CCV52592_0358.
DR KEGG; ccv:CCV52592_0358; -.
DR HOGENOM; CLU_003601_3_3_7; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006380; 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_1000068789"
FT BINDING 60..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 550 AA; 59241 MW; C88B170DDC4A8D78 CRC64;
MLSDIEITHL AKLDHISKIG AKLGLGEDDM ELYGKFKAKI EPRLDGSNSK LILVTATSPT
PFGEGKTTMS IGLADALNRL VKKVCLALRE PSLGPVFGIK GGAAGGGYSQ LAPMEDLNLH
FTGDFHAITS ANNLISAMID NSLYQENPLN IDKILWKRCM DMNDRALRFI TVGQGGKADG
VEREDGFNIT AASEIMAILC LATSLADLKE RIANIMVAYN DRGEPIYVRD LGCEDAVCIL
LKDAMKPNLF QTIEHTPTLV HGGPFANIAH GCNSIIATKT ALNLADFVIT EAGFGSELGA
EKFIDIKCRV AGIAPDAVVL VSTIRSLKYN GGADKESITK PNMSALEVGI ANLGGHIENL
KQKFGLNVVV ALNKFGFDED SEIDFVRDYC AKFGVKMAVC ENFVKGGEGA LELANFVLEE
LKKPNDMKFA YETSDDTKSK ITKIATEIYG AGEVVFEEAA QKALEKIKKL GLEKLPVCIA
KTQYSFSDDA KLLGRAKGFK FSVKDLQIRT GAGFIVAVCG KIMLMPGLPK TPSALNMHID
TKTGEISGLA
