ID MQO_ECO45 Reviewed; 548 AA. AC B7MFC3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 28-JAN-2026, entry version 88. 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}; GN OrderedLocusNames=ECS88_2358; OS Escherichia coli O45:K1 (strain S88 / ExPEC). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=585035; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S88 / ExPEC; 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CU928161; CAR03639.1; -; Genomic_DNA. DR RefSeq; WP_000758066.1; NC_011742.1. DR AlphaFoldDB; B7MFC3; -. DR SMR; B7MFC3; -. DR KEGG; ecz:ECS88_2358; -. DR HOGENOM; CLU_028151_0_0_6; -. DR UniPathway; UPA00223; UER01008. DR Proteomes; UP000000747; Chromosome. DR GO; GO:0047545; F:(S)-2-hydroxyglutarate dehydrogenase activity; IEA:TreeGrafter. DR GO; GO:0008924; F:L-malate dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule. DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR HAMAP; MF_00212; MQO; 1. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR006231; MQO. DR NCBIfam; TIGR01320; mal_quin_oxido; 1. DR NCBIfam; NF003603; PRK05257.1-1; 1. DR NCBIfam; NF003605; PRK05257.1-4; 1. DR NCBIfam; NF003606; PRK05257.2-1; 1. DR NCBIfam; NF003608; PRK05257.2-4; 1. DR NCBIfam; NF003611; PRK05257.3-2; 1. DR NCBIfam; NF009875; PRK13339.1; 1. DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43104:SF2; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1. DR Pfam; PF06039; Mqo; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. PE 3: Inferred from homology; KW FAD; Flavoprotein; Oxidoreductase; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1..548 FT /note="Probable malate:quinone oxidoreductase" FT /id="PRO_1000191314" FT REGION 521..548 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 530..541 FT /note="Low complexity" 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 //