MQO_PECCP
ID MQO_PECCP Reviewed; 527 AA.
AC C6DAM1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
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=PC1_2825;
OS Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=561230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Balakrishnan V., Glasner J., Perna N.T.;
RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001657; ACT13855.1; -; Genomic_DNA.
DR RefSeq; WP_015841015.1; NC_012917.1.
DR AlphaFoldDB; C6DAM1; -.
DR STRING; 561230.PC1_2825; -.
DR EnsemblBacteria; ACT13855; ACT13855; PC1_2825.
DR KEGG; pct:PC1_2825; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_028151_0_0_6; -.
DR OMA; PHLDTRW; -.
DR OrthoDB; 1371190at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000002736; 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 Gene3D; 3.50.50.60; -; 1.
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..527
FT /note="Probable malate:quinone oxidoreductase"
FT /id="PRO_1000204202"
SQ SEQUENCE 527 AA; 58178 MW; A323FC4E3E75B4B3 CRC64;
MKKLLAMFFC LTVVVNAPLA MAEDAKTTEK TTDVVLIGGG IMSSTLGVYL QELQPDWSID
MVERMDNVAE ESSNGWNNAG TGHSAFMELN YTPDNPDGPI NISKALEITE AFEVSRQFWS
YQVKNGVLNN PHSFINSVPH ISFVWGDENT AFLKHRYDAM QHSTLYRGME FSDDPNTIKE
WAPLVMEGRD PAQKIAATRM PIGTDVNYGE ITRQLVDAMK TKSNFALHLN SEVRDIKRNA
DNTWSVTYAD LKNGEKESVI KAKFVFIGAG GAALQLLQKT GIPEADLYGG FPVGGEFLVT
ENPEIVKRHM AKVYGKASVG APPMSVPHLD TRIFDGKPVL LFGPFATFSS KFLKNGSLWD
LIGSVTFSNV MPMTHVGLDN FDLVKYLIGQ VMMDDDDRFA SLKEYFPNAK KEDWRLTVAG
QRVQIIKKDD DKGGVLKLGT EIVSSQDGSI AALLGASPGA STAAPIMLSL LEKVFKDKVA
TPEWQSKLKE IVPSYGQKLD GNIEMTNKIR SYTSSTLGLD YIEVKPE