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
//