FTHS_PETMO
ID FTHS_PETMO Reviewed; 554 AA.
AC A9BIV8;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Pmob_1756;
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogae; Petrotogales; Petrotogaceae; Petrotoga.
OX NCBI_TaxID=403833;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95;
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., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-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; CP000879; ABX32446.1; -; Genomic_DNA.
DR RefSeq; WP_012209543.1; NC_010003.1.
DR AlphaFoldDB; A9BIV8; -.
DR SMR; A9BIV8; -.
DR STRING; 403833.Pmob_1756; -.
DR EnsemblBacteria; ABX32446; ABX32446; Pmob_1756.
DR KEGG; pmo:Pmob_1756; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_0; -.
DR OMA; CGEIMTM; -.
DR OrthoDB; 177859at2; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000789; 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..554
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000087653"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 554 AA; 60679 MW; 1C527EF6D73AB44A CRC64;
MLSDIEIARS AKLKKIDLIA NELDIPEEYY NLYGKNIAKV SHKYLNELNF KNDGNLVMVT
AITPTPAGEG KTTTSISLSM ALNKIHKRSI VTLREPSLGP VMGIKGGAAG GGYSQVLPME
DINLHFTGDI HAVTSAHNLI SAILDDYIKY NKYDIDSTQV SWPRTMDMND RALREIIVAL
GGKKNGYPRQ DGFIITAASE IMAILCLIEN LEDLKKKLSN IVVAKNKKGE PVTVKDLEIT
GALSVLLKDA INPNLVQTIE NTPAFVHGGP FANIAHGTNS ILATKLALKL SDYVVTETGF
GSDLGGEKFY DFVSPTFGLK PSATVLVATI RALKYHGGQN LKDLNTPNLE SLEKGLPNLQ
VHVENLKKYN IPVVVSLNKF YSDTDEEINM VKDYCDKLGV EVSVNEGFEK GSEGAIDLAE
KVVKVSEQQS ELKSIYDFKD PLEVKIEKLA KNIYRASKVE YSSEALSTIK FLKKYGYENL
PVIVAKTQYS ISDDPKKLGF PKDYTFTIRD FELSAGAGFI VALAGDILRM PGLSKVPNAV
NMDIDNEGNI SGLS
