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MQO_ESCF3
ID   MQO_ESCF3               Reviewed;         548 AA.
AC   B7LMB2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=EFER_0950;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(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; CU928158; CAQ88485.1; -; Genomic_DNA.
DR   RefSeq; WP_000758036.1; NC_011740.1.
DR   AlphaFoldDB; B7LMB2; -.
DR   PRIDE; B7LMB2; -.
DR   EnsemblBacteria; CAQ88485; CAQ88485; EFER_0950.
DR   GeneID; 60904089; -.
DR   KEGG; efe:EFER_0950; -.
DR   HOGENOM; CLU_028151_0_0_6; -.
DR   OMA; PHLDTRW; -.
DR   OrthoDB; 1371190at2; -.
DR   BioCyc; EFER585054:EFER_RS04865-MON; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000000745; 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_1000191317"
FT   REGION          522..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   548 AA;  60022 MW;  54705EF62BD3E552 CRC64;
     MKKVTAMLFS MAVGLNAGSA AAKAKASEEQ ETDVLLIGGG IMSATLGTYL RELEPEWSMT
     MVERLDSVAQ ESSNGWNNAG TGHSALMELN YTPQNADGSI SIEKAVAINE AFQISRQFWA
     HQVERGVLRT PRSFINTVPH MSFVWGEDNV NFLRARYAAL QQSSLFRGMR YSEDHEQIKE
     WAPLVMEGRD PQQKVAATRT EIGTDVNYGE ITRQLIASLQ KKSNFSLQLS SEVRALKRNG
     DKSWTVTIAD LKNGTVHNIR AKFVFIGAGG AALKLLQESG IPEAKDYAGF PVGGQFLVSE
     NPDVVNHHLA KVYGKASVGA PPMSVPHIDT RVLDGKRVVL FGPFATFSTK FLKNGSLWDL
     MSSTTTSNVL PMMHVGLDNF DLVKYLISQV MLSEDDRFAA LKEYYPQAKK EDWRLWQAGQ
     RVQIIKRDAD KGGVLRLGTE VVSDQQGTIA ALLGASPGAS TAAPIMLNLL EKVFGDRVSS
     PQWQATLKAI VPSYGSKLNG NVAATERELQ YTSEVLGLKY DKPQAADSTP KAQLKPQPAR
     KEVADIAL
 
 
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