FTHS_SYNWW
ID FTHS_SYNWW Reviewed; 555 AA.
AC Q0AX38;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Swol_1409;
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(2010).
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; CP000448; ABI68716.1; -; Genomic_DNA.
DR RefSeq; WP_011640815.1; NC_008346.1.
DR AlphaFoldDB; Q0AX38; -.
DR SMR; Q0AX38; -.
DR STRING; 335541.Swol_1409; -.
DR EnsemblBacteria; ABI68716; ABI68716; Swol_1409.
DR KEGG; swo:Swol_1409; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000001968; 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..555
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300551"
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; 59492 MW; FCDEFF5E102A9BFA CRC64;
MKTDVEIAQS AKMQPITEIA DRIGIEPNEL ELYGSYKAKI SLDIMKRIED KPQGKLVLVT
AISPTPAGEG KTTTTIGLGQ ALNKIGKKAI VALREPSLGP VFGIKGGATG GGYAQVVPME
DINLHFTGDI HAVTTAHNLL AALMDNHLHQ GNELDIDSRQ IVWRRVMDLN ERVLRNIVLG
LGGRINGVPR ESGFDISVAS EVMAALCLAT DLMDLKERFA KIVVAYSQQG QAITAGDLKA
AGSMALLMKD AIKPNLVQTL ENTPAFIHGG PFANIAHGAN SIVATRLGVK LADYMVTEAG
FGADLGAEKF FNIVCRYGKL VPDAVVLVAS IRALKHHGGV KKDKLGEENL EALAQGMENL
KKHLENIQKF GVPAVVALNE FPSDTSKEID YVFSQCAAMQ TAVSISRVWA QGGEGGIDLA
EKLVLATEQG SQFKFLYELN QPLKNKIETI CREIYGAGSV KYAAEAKRML QKYEESGFGD
LPVCIAKTQY SLSDNAQLLG RPTGFEVNIR QVKLSAGAGF VVALAGDIMT MPGLGKVPAA
ENIDIKPDGE IVGLF
