FTHS_THEPX
ID FTHS_THEPX Reviewed; 555 AA.
AC B0K5A5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Teth514_0795;
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter;
OC unclassified Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-2008) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000923; ABY92098.1; -; Genomic_DNA.
DR RefSeq; WP_009052988.1; NC_010320.1.
DR AlphaFoldDB; B0K5A5; -.
DR SMR; B0K5A5; -.
DR PRIDE; B0K5A5; -.
DR EnsemblBacteria; ABY92098; ABY92098; Teth514_0795.
DR KEGG; tex:Teth514_0795; -.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; TRQGFSK; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002155; 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_1000146707"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 555 AA; 60378 MW; E6AB1DF55C49FC23 CRC64;
MKSDIEIAQE AKMLHIREVA KKLDIEEDYL EYYGKYKAKI SPALSEKIKD RKDGKLILVT
AITPTPAGEG KTTLTVGLGQ ALAKIGKKAM IALREPSLGP CMGIKGGAAG GGYSQVVPME
DINLHFTGDL HAITAAHNLL AAMIDNHIHH GNELNIDIRA ITWKRAMDMN DRALREIIVG
LGGKANGFPR QDGFIITVAS EVMAILCLAQ DLMDLKRRIG DIIVAYDKDG NPVTARDLKA
DGAMTVLLKD AIKPNLVQTI ENVPAFVHGG PFANIAHGCN SLIATKYGLK LADYLVTEAG
FGADLGAEKF FDIKSRFGGL TPNAAVIVAT VRALKMHGGV KKEDLQKEDV EAVRRGIENL
EKQVENVRKF GVPVVVALNR FVFDTEREIE EVRKACEEMG VDMAVAEVWE KGGEGGIELA
EKVVKACETP SNFHVLYDET LPIKDKLHII ATEIYGADGV EYTASALKDI ANLERLGFDK
MPIVVAKTQY SLSDDPKLLG RPRGFKITVR ELRVSMGAGF VVVFTGDIMT MPGLPKHPAA
ENIDIDENGR ITGLF