ID   MQO_ECOK1               Reviewed;         548 AA.
AC   A1AD63;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=Ecok1_21090;
GN   ORFNames=APECO1_4349;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ01603.1; -; Genomic_DNA.
DR   RefSeq; WP_000758066.1; NC_008563.1.
DR   AlphaFoldDB; A1AD63; -.
DR   EnsemblBacteria; ABJ01603; ABJ01603; APECO1_4349.
DR   GeneID; 58462674; -.
DR   KEGG; ecv:APECO1_4349; -.
DR   HOGENOM; CLU_028151_0_0_6; -.
DR   OMA; PHLDTRW; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000008216; 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..548
FT                   /note="Probable malate:quinone oxidoreductase"
FT                   /id="PRO_1000023798"
FT   REGION          521..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  60230 MW;  2378A6D125EBB238 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
     RVQIIKRDAD KGGVLRLGTE VVSDQQGTIA ALLGASPGAS TAAPIMLNLL EKVFGDRVSS
     PQWQATLKAI VPSYGRKLNG DVAATERELQ YTSEVLGLKY DKPQAADSTP KPQLKPQPVQ
     KEVADIAL