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L2HDH_CAEBR
ID   L2HDH_CAEBR             Reviewed;         434 AA.
AC   A8X2R1; E3CTZ3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial;
DE            EC=1.1.99.2;
DE   Flags: Precursor;
GN   ORFNames=CBG06643;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2;
CC         Xref=Rhea:RHEA:21252, ChEBI:CHEBI:13193, ChEBI:CHEBI:16782,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the L2HGDH family. {ECO:0000305}.
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DR   EMBL; HE601320; CBX33056.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8X2R1; -.
DR   SMR; A8X2R1; -.
DR   STRING; 6238.CBG06643; -.
DR   EnsemblMetazoa; CBG06643.1; CBG06643.1; WBGene00028888.
DR   WormBase; CBG06643; CBP37606; WBGene00028888; -.
DR   eggNOG; KOG2665; Eukaryota.
DR   HOGENOM; CLU_024775_0_0_1; -.
DR   InParanoid; A8X2R1; -.
DR   OMA; GVHFTRM; -.
DR   OrthoDB; 1310154at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IBA:GO_Central.
DR   GO; GO:0047545; F:2-hydroxyglutarate dehydrogenase activity; IBA:GO_Central.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01266; DAO; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..434
FT                   /note="L-2-hydroxyglutarate dehydrogenase, mitochondrial"
FT                   /id="PRO_0000331210"
SQ   SEQUENCE   434 AA;  48359 MW;  52C3C2C688BF6977 CRC64;
     MLTRKTFHAF RSISGPPKKS VELPKYDLVI VGGGIVGCAT ARQLLIEKPN LKIALVEKEK
     ELAVHQSGHN SGVIHAGIYY TPGSLKAKLC VEGLDLSYEF FDKEKIPYKK TGKLIVAVEQ
     EEVPRLDALF ARAQTNGCRD IEMIDSKRIT DIEPHCKGLK ALWSPHTGIV DWGYVTKKFG
     EDFEKRGGKI YTSYPLEKIE DNLKDSNYPI RVSSDPSYAD FETKNLITCA GLQSDRVAAL
     SGCSTDPKIV PFRGEYLLLK PEKRHLVKTN IYPVPDPRFP FLGVHFTPRM NGDIWLGPNA
     VLAYKREGYS YFSISPSDLL ESLSYSGMQK LVKKHFTFGI KELYRGIWIA AQVKQLQRFI
     PELKYSDVTR GPSGVRAQAM DSAGNLVDDF VFDSGTGKLS SLIMHVRNAP SPAATSSLAI
     AKMITSEAIT RFKL
 
 
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