ID   MQO_ECOBW               Reviewed;         548 AA.
AC   C4ZU53;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=BWG_1984;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(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; CP001396; ACR63707.1; -; Genomic_DNA.
DR   RefSeq; WP_000758077.1; NC_012759.1.
DR   AlphaFoldDB; C4ZU53; -.
DR   PRIDE; C4ZU53; -.
DR   KEGG; ebw:BWG_1984; -.
DR   HOGENOM; CLU_028151_0_0_6; -.
DR   OMA; PHLDTRW; -.
DR   UniPathway; UPA00223; UER01008.
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..548
FT                   /note="Probable malate:quinone oxidoreductase"
FT                   /id="PRO_1000204197"
FT   REGION          521..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  60230 MW;  3278A6D124EEE2AA CRC64;
     MKKVTAMLFS MAVGLNAVSM AAKAKASEEQ ETDVLLIGGG IMSATLGTYL RELEPEWSMT
     MVERLEGVAQ ESSNGWNNAG TGHSALMELN YTPQNADGSI SIEKAVAINE AFQISRQFWA
     HQVERGVLRT PRSFINTVPH MSFVWGEDNV NFLRARYAAL QQSSLFRGMR YSEDHAQIKE
     WAPLVMEGRD PQQKVAATRT EIGTDVNYGE ITRQLIASLQ KKSNFSLQLS SEVRALKRND
     DNTWTVTVAD LKNGTAQNIR AKFVFIGAGG AALKLLQESG IPEAKDYAGF PVGGQFLVSE
     NPDVVNHHLA KVYGKASVGA PPMSVPHIDT RVLDGKRVVL FGPFATFSTK FLKNGSLWDL
     MSSTTTSNVM PMMHVGLDNF DLVKYLVSQV MLSEEDRFEA LKEYYPQAKK EDWRLWQAGQ
     RVQIIKRDAE KGGVLRLGTE VVSDQQGTIA ALLGASPGAS TAAPIMLNLL EKVFGDRVSS
     PQWQATLKAI VPSYGRKLNG DVAATERELQ YTSEVLGLNY DKPQAADSTP KPQLKPQPVQ
     KEVADIAL