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MQO_ACIAD
ID   MQO_ACIAD               Reviewed;         543 AA.
AC   Q6FDG0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=ACIAD1007;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG67898.1; -; Genomic_DNA.
DR   RefSeq; WP_004921803.1; NC_005966.1.
DR   AlphaFoldDB; Q6FDG0; -.
DR   STRING; 62977.ACIAD1007; -.
DR   EnsemblBacteria; CAG67898; CAG67898; ACIAD1007.
DR   GeneID; 45233453; -.
DR   KEGG; aci:ACIAD1007; -.
DR   eggNOG; COG0579; Bacteria.
DR   HOGENOM; CLU_028151_0_0_6; -.
DR   OMA; PHLDTRW; -.
DR   OrthoDB; 1371190at2; -.
DR   BioCyc; ASP62977:ACIAD_RS04640-MON; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000000430; 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; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..543
FT                   /note="Probable malate:quinone oxidoreductase"
FT                   /id="PRO_1000023789"
SQ   SEQUENCE   543 AA;  60682 MW;  F8F5A79EA4DBC168 CRC64;
     MKKFLKYLAV FLVVLLIAAI AFLFRPIASK KIQTSANEPV VDVVLVGGGI MSATLGTYLT
     ELEPNWQIRM YERLDRVAQE SSNGFNNAGT GHSGFMEMNY TEEKDGKMDI SKAVKVAEQF
     EISKQFWAYQ VKHNVLGQPS SFINPVPHHA FVWGDNVAFL EKRYAAMIKN PLFYGMQFTE
     NANQIKQWAP LTMEGRDPAQ KVAATRMEIG SDVNYGAITT QLVNNLDKHQ NFKLSTSSEV
     TGISQNDDKT WTVAFKNLKT GKADHVKTRF VFIGAGGASV KLLQMTGLPE SKQYAGFPVG
     GVFLMTDNPK IAAEHTAKLY GRAELGAPPM SVPHIDTRYI DGKKYVLFGP FATYSNKFLK
     QGSQFDLLAS TNKNNVLPMT AVGMENLDLV KYLVSQVMMT DEDRFNELKK YYPNAKREDW
     RLNQGGQRVQ VIKKEEGKPA KLQFGTEVFV SKDRSVTALM GASPGASTSP YIMLNLLEKA
     FPQQVKGEWN PKLHEIVRSY KQDLSDNPVL LDQVRQYTSQ TLGLHYTPLT QADFAKIAAS
     QSK
 
 
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