FTHS_LACLA
ID FTHS_LACLA Reviewed; 555 AA.
AC Q9CH07;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=LL0935;
GN ORFNames=L159505;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
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; AE005176; AAK05033.1; -; Genomic_DNA.
DR PIR; G86741; G86741.
DR RefSeq; NP_267091.1; NC_002662.1.
DR RefSeq; WP_010905639.1; NC_002662.1.
DR AlphaFoldDB; Q9CH07; -.
DR SMR; Q9CH07; -.
DR STRING; 272623.L159505; -.
DR PaxDb; Q9CH07; -.
DR EnsemblBacteria; AAK05033; AAK05033; L159505.
DR KEGG; lla:L159505; -.
DR PATRIC; fig|272623.7.peg.1000; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; CGEIMTM; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000002196; 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_0000199355"
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; 59443 MW; BEF24F56C1B259A1 CRC64;
MKTDIEIAQA ADIQPITKIA EKIGLSFDDI ELYGKYKAKI PLEVLDKFDQ QSEGKLVLVT
SINPTPAGEG KSTVTVGLAD AFARQGKNVM VALREPSLGP VMGIKGGAAG GGFAQVLPME
DINLHFTGDI HAITTANNAI SAFLDNSLHQ GNPLNIDPRR IIWKRVVDLN DRALRHVTVG
LGGPLNGVPR EDGFDITVVS EIMAVLCLAT SISDLKERLG KIVLAQSYDR KPVTLGDLGV
QGAIAMLLKD ALKPNLVQTI EGTPALIHGG PFANIAHGCN SVLATKTALK LSDIVITEAG
FGADLGGEKF LDIKTRQLGK QPDAVVIVAT LRALKMHGGL DKKELTKENV EAVKKGFANL
ERHIKNMQSY GLPVIVAINE FASDTKSEIS ALKDLTEALG VPVSLTQVFA KGGEGGLDLA
EKLSGMLQEK SDFSYLYDLK EPLSAKIDKV VTEIYGGSKV NYSPKAKRQM REIEENGWND
LPVCMAKTQY SFSDQPNLLA APEGFEVTVR ELLPKIGAGF IVALLGDVMT MPGLPKNPAS
LKMDVTDDGK ISGLF
