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FTHS_SYMTH
ID   FTHS_SYMTH              Reviewed;         556 AA.
AC   Q67JH9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=STH3189;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD42171.1; -; Genomic_DNA.
DR   RefSeq; WP_011197302.1; NC_006177.1.
DR   AlphaFoldDB; Q67JH9; -.
DR   SMR; Q67JH9; -.
DR   STRING; 292459.STH3189; -.
DR   EnsemblBacteria; BAD42171; BAD42171; STH3189.
DR   KEGG; sth:STH3189; -.
DR   eggNOG; COG2759; Bacteria.
DR   HOGENOM; CLU_003601_3_3_9; -.
DR   OMA; TRQGFSK; -.
DR   OrthoDB; 177859at2; -.
DR   UniPathway; UPA00193; -.
DR   Proteomes; UP000000417; 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..556
FT                   /note="Formate--tetrahydrofolate ligase"
FT                   /id="PRO_0000199401"
FT   BINDING         65..72
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01543"
SQ   SEQUENCE   556 AA;  59450 MW;  49822EE6AAD9BDAE CRC64;
     MLSDIAIAQR ARLEPITKVA EQIGLGPEDL ELYGRYKAKV ADHVWPRVRS NPDGKLILVT
     AISPTPAGEG KTTVTVGLGQ AMSRIGKRAI IALREPSLGP AFGVKGGAAG GGYSQVVPMD
     EINLHFTGDF HAVTAANNLL AAMIDNHLHQ GNKLGLDPRQ ITFKRVLDMN DRALRSVVIG
     LGGKNGGVPR QEEFMITPAS EVMATLCLAE DLADLKRRCG EIIVGYTYDG APVRARDLKA
     EGAMATLLKE AIKPNLVQTL ENTPAFVHGG PFANIAHGCN TVVATRLALK LADYVITEAG
     FGADLGAEKF IDIKCRLSGL RPDAVVVVAT IRSLKMHGGL KKDDLAREDL EALQRGSANL
     MRHLRNVTEV FGLPAVVAIN RFAADTEAEI ALLRALVEEA GATAVVADVH ARGGDGGIEL
     AQRVVELVEQ PNRFRFAYDD EDSLKTKIEK VATRIYGADG VDFTREASRM LKKLESEGFG
     RAPVCIAKTQ YSFSDDPKKL GAPTGWRLTV REVRPSAGAG FVVALTGEIM TMPGLPPVPA
     AESIDVSDDG EITGLF
 
 
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