FTHS_DESPS
ID FTHS_DESPS Reviewed; 557 AA.
AC Q6AL19;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-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=DP2227;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(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; CR522870; CAG36956.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6AL19; -.
DR SMR; Q6AL19; -.
DR STRING; 177439.DP2227; -.
DR EnsemblBacteria; CAG36956; CAG36956; DP2227.
DR KEGG; dps:DP2227; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_7; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000602; 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..557
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000199346"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 557 AA; 60188 MW; 1D4E4CE5390AEF03 CRC64;
MDLTKEEILP YGHHVAKLDY RKILDRCADR PDGKYIDVTA ITPTPLGEGK STSVMGLVQG
LGKRDKSVVG AIRQPSGGPT MNIKGSAAGG GRSQCIPLNE FSLGLTGDIN SIMNAHNLGM
VALTARMQHE ANYTDAQLAQ RNLKRLDIHP KKIQFSWIID FCAQALRNIT IGIGGKMDGP
TIQSSFAIAV SSELMAILAI ANDLADMRAR IAKVVVAYDK QDRPITTADL EVDGAMTAWM
VQAINPNLMQ TLEGQPVLVH AGPFANIAIG QSSVIADRVG LKIAGYNVTE SGFGADIGFE
KFWNLKCRFS GNKPNCAVIV ATIRALKCHG GAPIPVPGKP MPEEYAKENV GWVEEGCKNL
LHHINTVKKA GINPVVCINA FYTDRPNEIK AVKRICEHAG ARVAVSTHWE HGGDGALEFA
DAVIDACEEK NDFKFLYELD TPLEKRIELI AKEVYGADGV SYTPEARTKL TQLAKDPEMA
ELGTCMVKTH LSLSHDPKLK GVPKGWTLPI RDILTYKGAG FVVPVAGAIS LMPGTGSDPA
YRRVDVDLQT GRVKGVF
