FTHS_METEP
ID FTHS_METEP Reviewed; 557 AA.
AC A9VZT0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Mext_0414;
OS Methylorubrum extorquens (strain PA1) (Methylobacterium extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=419610;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA1;
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., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Marx C., Richardson P.;
RT "Complete sequence of Methylobacterium extorquens PA1.";
RL Submitted (DEC-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; CP000908; ABY28836.1; -; Genomic_DNA.
DR RefSeq; WP_012252208.1; NC_010172.1.
DR AlphaFoldDB; A9VZT0; -.
DR SMR; A9VZT0; -.
DR STRING; 419610.Mext_0414; -.
DR EnsemblBacteria; ABY28836; ABY28836; Mext_0414.
DR KEGG; mex:Mext_0414; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_5; -.
DR OMA; CGEIMTM; -.
DR BioCyc; MEXT419610:MEXT_RS02055-MON; -.
DR UniPathway; UPA00193; -.
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..557
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_1000196814"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 557 AA; 59462 MW; F69B51A63A4D0819 CRC64;
MPSDIEIARA ATLKPIAQVA EKLGIPDEAL HNYGKHIAKI DHDFIASLEG KPEGKLVLVT
AISPTPAGEG KTTTTVGLGD ALNRIGKRAV MCLREPSLGP CFGMKGGAAG GGKAQVVPME
QINLHFTGDF HAITSAHSLA AALIDNHIYW ANELNIDVRR IHWRRVVDMN DRALRAINQS
LGGVANGFPR EDGFDITVAS EVMAVFCLAK NLADLEERLG RIVIAETRDR KPVTLADVKA
TGAMTVLLKD ALQPNLVQTL EGNPALIHGG PFANIAHGCN SVIATRTGLR LADYTVTEAG
FGADLGAEKF IDIKCRQTGL KPSAVVIVAT IRALKMHGGV NKKDLQAENL DALEKGFANL
ERHVNNVRSF GLPVVVGVNH FFQDTDAEHA RLKELCRDRL QVEAITCKHW AEGGAGAEAL
AQAVVKLAEG EQKPLTFAYE TETKITDKIK AIATKLYGAA DIQIESKAAT KLAGFEKDGY
GKLPVCMAKT QYSFSTDPTL MGAPSGHLVS VRDVRLSAGA GFVVVICGEI MTMPGLPKVP
AADTIRLDAN GQIDGLF