FTHS1_LACAC
ID FTHS1_LACAC Reviewed; 558 AA.
AC Q5FJY2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Formate--tetrahydrofolate ligase 1 {ECO:0000255|HAMAP-Rule:MF_01543};
DE EC=6.3.4.3 {ECO:0000255|HAMAP-Rule:MF_01543};
DE AltName: Full=Formyltetrahydrofolate synthetase 1 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FHS 1 {ECO:0000255|HAMAP-Rule:MF_01543};
DE Short=FTHFS 1 {ECO:0000255|HAMAP-Rule:MF_01543};
GN Name=fhs1 {ECO:0000255|HAMAP-Rule:MF_01543}; OrderedLocusNames=LBA1153;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV42992.1; -; Genomic_DNA.
DR RefSeq; WP_011254358.1; NC_006814.3.
DR RefSeq; YP_194023.1; NC_006814.3.
DR AlphaFoldDB; Q5FJY2; -.
DR SMR; Q5FJY2; -.
DR STRING; 272621.LBA1153; -.
DR PRIDE; Q5FJY2; -.
DR EnsemblBacteria; AAV42992; AAV42992; LBA1153.
DR GeneID; 56942754; -.
DR KEGG; lac:LBA1153; -.
DR PATRIC; fig|272621.13.peg.1094; -.
DR eggNOG; COG2759; Bacteria.
DR HOGENOM; CLU_003601_3_3_9; -.
DR OMA; VDNYIYQ; -.
DR BioCyc; LACI272621:G1G49-1143-MON; -.
DR UniPathway; UPA00193; -.
DR Proteomes; UP000006381; 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 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.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Nucleotide-binding; One-carbon metabolism;
KW Reference proteome.
FT CHAIN 1..558
FT /note="Formate--tetrahydrofolate ligase 1"
FT /id="PRO_0000199351"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ SEQUENCE 558 AA; 60595 MW; E5F4B694A0176CA1 CRC64;
MKSDIEIAQE TKELPIEEIA AKVNLKKEDL EPYGQDKAKI NWKAINRIRK NDKLGKLILV
TSISPTPAGE GKSTITIGLG DAIHNQLHKN TLIALREPSM GPVFGLKGGA TGGGRAQIIP
MEDINLHFTG DMHALTAAID TLAALVDNYI YQDNSLNIDP ERILLKRGLD VNDRALRKIT
VGQGSKFNGI EHKASFAITV ANELMAILCL ANDINDLKAR IGDMLVGYTQ DDQPVYVKQL
GFQGAIAALL SNALKPNLVQ TLEHTPALVH GGPFANIAHG ANSVMATNLA LHLSDYVLTE
AGFGSDLGGQ KFMDFVSKHL DKTPDAAVVV ATVRALKYQA LGSTDKLDEE NLDALKTGFK
NLERHMNNMR SYNVPVIVLI NRFDTDTDKE LELLKELVEK QGIKAEVVTY HNEGSKGGSR
AAQEVINLAD SGKAELISTY NEDDDIKSKI KKIATKIYHA DGVEYTDKAE EQIKELAKIG
KDKLPVIIAK TQYSFSDDKK KLGAPGGFNL HVKGVSLKNG ARFIVVTTGN VLDMPGLPKH
PAALDIDVDN DGKISGLF