FTHS_PSELT
ID FTHS_PSELT Reviewed; 553 AA.
AC A8F7D5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, 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=Tlet_1513;
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Pseudothermotoga.
OX NCBI_TaxID=416591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO;
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., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-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; CP000812; ABV34069.1; -; Genomic_DNA.
DR RefSeq; WP_012003545.1; NC_009828.1.
DR AlphaFoldDB; A8F7D5; -.
DR SMR; A8F7D5; -.
DR STRING; 416591.Tlet_1513; -.
DR EnsemblBacteria; ABV34069; ABV34069; Tlet_1513.
DR KEGG; tle:Tlet_1513; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_0; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002016; 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..553
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000068797"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 553 AA; 59366 MW; 4A5F59E26DF224C2 CRC64;
MLSDIEIARS AKLEPVMNIA KNLSIPGDFL NSYGKFMAKI SHSFLKNLNI RKGKLILVTA
MTPTPAGEGK TTTSIGLSMA LNKIGHRSIV TLREPSLGPV FGIKGGAAGG GYSQVLPMED
INLHFTGDIH AVGTAHNLIS AVIDSHIRFG NDLDIDLTKI TWPRAIDMND RALRNIVIAL
GGHANGYPRE DGFVITAASE IMAILCLSKD LQDLKNRVGN IVIGWSKNGK PVTVHELGIE
GAIAVILKDA INPNLVQTIE NTPAFIHGGP FANIAHGTNS IIATKMALGL SDYVVTESGF
GSDLGAEKFF DFVSPAADLK PSVAVIVATV RAIKYHGGVP LKDLENENLE AIKKGIENLK
IHIENVKKFN VPVVVALNRF ATDTERELDL VVNTVEKLGT KISLNEAFAK GSEGAIDLAK
KVIEVADESK FSPIYKWDSP VEEKIKILAT EIYRAKDVSF SKEAITSLKQ IEKAGLSNLP
VIVAKTQYSI SDDPSKLGAP DGYVFNVRNF KLSSGAGFIV AISGEIMLMP GLGKKPNAVN
IDIDEKGNIT GLF