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Database: UniProt
Entry: A0A1D8YCJ6_9GAMM
LinkDB: A0A1D8YCJ6_9GAMM
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ID   A0A1D8YCJ6_9GAMM        Unreviewed;       563 AA.
AC   A0A1D8YCJ6;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Probable malate:quinone oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00212};
DE            EC=1.1.5.4 {ECO:0000256|HAMAP-Rule:MF_00212};
DE   AltName: Full=MQO {ECO:0000256|HAMAP-Rule:MF_00212};
DE   AltName: Full=Malate dehydrogenase [quinone] {ECO:0000256|HAMAP-Rule:MF_00212};
GN   Name=mqo {ECO:0000256|HAMAP-Rule:MF_00212};
GN   ORFNames=BIZ42_14585 {ECO:0000313|EMBL:AOX63316.1};
OS   Stenotrophomonas sp. LM091.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=1904944 {ECO:0000313|EMBL:AOX63316.1, ECO:0000313|Proteomes:UP000177427};
RN   [1] {ECO:0000313|EMBL:AOX63316.1, ECO:0000313|Proteomes:UP000177427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LM091 {ECO:0000313|EMBL:AOX63316.1,
RC   ECO:0000313|Proteomes:UP000177427};
RA   Lefeuvre P.;
RT   "Complete genome sequence of a copper-resistant commensal bacteria:
RT   Stenotrophomonas sp. strain LM091.";
RL   Submitted (SEP-2016) 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:0000256|ARBA:ARBA00001139, ECO:0000256|HAMAP-
CC         Rule:MF_00212};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|HAMAP-Rule:MF_00212};
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       oxaloacetate from (S)-malate (quinone route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00005012, ECO:0000256|HAMAP-Rule:MF_00212}.
CC   -!- SIMILARITY: Belongs to the MQO family. {ECO:0000256|HAMAP-
CC       Rule:MF_00212}.
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DR   EMBL; CP017483; AOX63316.1; -; Genomic_DNA.
DR   RefSeq; WP_070426841.1; NZ_CP017483.1.
DR   AlphaFoldDB; A0A1D8YCJ6; -.
DR   STRING; 1904944.BIZ42_14585; -.
DR   KEGG; slm:BIZ42_14585; -.
DR   OrthoDB; 9763983at2; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000177427; 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; 3.30.9.10; 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   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 {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_00212};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW   Rule:MF_00212};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00212}; Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT   REGION          534..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   563 AA;  62049 MW;  C4BD47330F1D154D CRC64;
     MKKLAKVVLG LLVLLLLAAA LFLYWPLHQR SVPAAGNDKP VDVVLVGGGI MSITLATFLQ
     ELQPDWNIQV YERLDGVALE SSDGWNNAGT GHSAFAELNY TPELPDGSIE TKRAVGIAEQ
     FEISRQFWSH QVREGRLSQP SDFINPTPHM SFVWGDENIA YLHKRQQALV KNPLFYGMQY
     SEDAAQIKQW APLLMEGRDP KQKVAATWMP LGTDVNFGVI TRQLTAGLQR SPNFSLHLNH
     EVRALRQNDD KSWNVTVKDL KSDNESTVKS RFVFIGAGGA ALKLLQLSGI PESKNYAGFP
     VGGQFLAFQS PQVAGRHSVK AYGMAETGSP PMSVPHLDAR KLDGKPVVLF GPFALYSTKF
     LKHGSWFDLY SSVNHNNVAG MMGVGLENLD LVKYLMGQAR LNDDDRQAEL VKYYPNAKRE
     DWTLVTAGQR VQIIKKDPEK GSILQFGTEI VTDQDHTLAA LLGASPGAST SPPIMLDLLK
     KAFPEQMAAG WEARLKEIVP SYGRKLNDSP ALTNEIRRLT SDTLKLPYLD VPGETSPAVM
     LTPPPGTQPA EAKRNANEEL QAL
//
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