FTHS_LACLM
ID FTHS_LACLM Reviewed; 555 AA.
AC A2RLK1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=llmg_1595;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL98169.1; -; Genomic_DNA.
DR RefSeq; WP_011835425.1; NZ_WJVF01000018.1.
DR AlphaFoldDB; A2RLK1; -.
DR SMR; A2RLK1; -.
DR STRING; 416870.llmg_1595; -.
DR EnsemblBacteria; CAL98169; CAL98169; llmg_1595.
DR KEGG; llm:llmg_1595; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR PhylomeDB; A2RLK1; -.
DR BioCyc; LLAC416870:LLMG_RS08030-MON; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000000364; 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..555
FT /note="Formate--tetrahydrofolate ligase"
FT /id="PRO_0000300525"
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; 59516 MW; E137C8573039AE67 CRC64;
MKTDIEIAQA AEIQPITKIA EKIGLSFDDI ELYGKYKAKI PLEVLEKFDE QNDGKLVLVT
SINPTPAGEG KSTVTVGLAD AFARQDKNVM VALREPSLGP VMGIKGGAAG GGFAQVLPME
DINLHFTGDI HAITTANNAI SAFLDNSLHQ GNPLNIDPRR IIWKRVLDLN DRALRHVTIG
LGGPLNGVPR EDGFDITVAS EIMAVLCLAT SISDLKERLA RIVIAQNYDR KPVSVGDLGV
QGAIAMLLKD ALKPNLVQTI EGTPALIHGG PFANIAHGCN SVLATKTALK LADIVITEAG
FGADLGGEKF LDIKTRQLGK QPDAVVIVAT LRALKMHGGV DKKELTSENV EAVKKGFANL
ERHIKNMQSY GLPVIVAINQ FASDTESEIS TLKELTEALG VSVSLTQVFA KGGEGGLDLA
EKLSAMLQAK PDFRYLYELN QPLSVKLDKV VTEIYGGSKV NLSPKAKRQM REIEENGWNN
LPVCMAKTQY SFSDQANLLA APEGFEVTVR ELIPKIGAGF IVALLGDVMT MPGLPKNPAA
LKMDVTDDGK ISGLF
