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MQO_BACCQ
ID   MQO_BACCQ               Reviewed;         500 AA.
AC   B9J484;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Probable malate:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00212};
DE            EC=1.1.5.4 {ECO:0000255|HAMAP-Rule:MF_00212};
DE   AltName: Full=MQO {ECO:0000255|HAMAP-Rule:MF_00212};
DE   AltName: Full=Malate dehydrogenase [quinone] {ECO:0000255|HAMAP-Rule:MF_00212};
GN   Name=mqo {ECO:0000255|HAMAP-Rule:MF_00212}; OrderedLocusNames=BCQ_2795;
OS   Bacillus cereus (strain Q1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=361100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Q1;
RX   PubMed=19060151; DOI=10.1128/jb.01629-08;
RA   Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA   Xue Y., Zhu Y., Jin Q.;
RT   "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT   with industrial applications.";
RL   J. Bacteriol. 191:1120-1121(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + a quinone = a quinol + oxaloacetate;
CC         Xref=Rhea:RHEA:46012, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:132124; EC=1.1.5.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00212};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00212};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       oxaloacetate from (S)-malate (quinone route): step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00212}.
CC   -!- SIMILARITY: Belongs to the MQO family. {ECO:0000255|HAMAP-
CC       Rule:MF_00212}.
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DR   EMBL; CP000227; ACM13223.1; -; Genomic_DNA.
DR   RefSeq; WP_000069168.1; NC_011969.1.
DR   AlphaFoldDB; B9J484; -.
DR   EnsemblBacteria; ACM13223; ACM13223; BCQ_2795.
DR   GeneID; 64201581; -.
DR   KEGG; bcq:BCQ_2795; -.
DR   HOGENOM; CLU_028151_0_0_9; -.
DR   OMA; PHLDTRW; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000000441; Chromosome.
DR   GO; GO:0052589; F:malate dehydrogenase (menaquinone) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008924; F:malate dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00212; MQO; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR006231; MQO.
DR   Pfam; PF06039; Mqo; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01320; mal_quin_oxido; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..500
FT                   /note="Probable malate:quinone oxidoreductase"
FT                   /id="PRO_1000124765"
SQ   SEQUENCE   500 AA;  55195 MW;  A32251CFFE75347A CRC64;
     MSNMQQKTDV ILIGAGIMSA TLGSLLKELA PEWEIKVFEK LASAGEESSN EWNNAGTGHS
     ALCELNYTSE KSDGSIDISK AVKVNEQFQL SRQFWAYLVK SKLIRNPQDF IMPLPHMSLV
     QGEKNVQFLK NRFEALSKNP LFQGMEFSDS PETLKKWLPL IMEGRTSNEP MAATKIDSGT
     DVNFGALTRM LFDYLKTKNV ELNYKHSVEN IKRTKNGLWE VKVHDMNSGK IEHHTAKFVF
     IGGGGGSLPL LQKTGIPESK HIGGFPVSGL FMVCKNQKVV EQHHAKVYGK AKVGAPPMSV
     PHLDTRYIDN KKALLFGPFA GFSPKFLKTG SNLDLIGSVK PNNVLTMLAA GVKEMGLTKY
     LIQQVMLSHE KRMEELREFI PNAKSEDWDI VVAGQRVQVI KDTDAGGKGT LQFGTEVVSA
     ADGSIAALLG ASPGASTAVH VMLEVLEKCF PSRMVEWEGK IKEMIPSYGI SLTENPRLFQ
     DLHTSTGRTL GLNEKETVHN
 
 
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