ID A0A0M4QG02_9MICC Unreviewed; 497 AA.
AC A0A0M4QG02;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=AOC05_09770 {ECO:0000313|EMBL:ALE92530.1};
OS Arthrobacter alpinus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=656366 {ECO:0000313|EMBL:ALE92530.1, ECO:0000313|Proteomes:UP000062833};
RN [1] {ECO:0000313|Proteomes:UP000062833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R3.8 {ECO:0000313|Proteomes:UP000062833};
RA See-Too W.S., Chan K.G.;
RT "Complete genome of Arthrobacter alpinus strain R3.8.";
RL Submitted (SEP-2015) 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; CP012677; ALE92530.1; -; Genomic_DNA.
DR RefSeq; WP_062007053.1; NZ_CP012677.1.
DR AlphaFoldDB; A0A0M4QG02; -.
DR KEGG; aaq:AOC05_09770; -.
DR PATRIC; fig|656366.3.peg.2110; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000062833; 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}; Reference proteome {ECO:0000313|Proteomes:UP000062833};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ SEQUENCE 497 AA; 53894 MW; 089B7EBED4E18ACF CRC64;
MTFISTTKDA DVVLIGGGIM SATLGTMLKQ LEPSWKIVLF EQLDEPGLES SSPWNNAGTG
HSALCELNYS PAAKDGSVNP AKAIDINEQF QLSRQFWSHM VANKMIGSPK GFINTVPHMS
FVIGEDHRKF LKARHQALAP NPLFSSMEYT EDPAQIAKWA PLVMKGRDAT QKVSATRAAE
GTDVDFGALT RELMGYMDNN DVEINYGTSV SNVSRTTDGQ WDVALKYPKS GEHGKIKAKF
VFIGSGGGAL HLLQLSGIAE GKGFGGFPVS GQFFRCTDET LAKQHSAKVY GQASVGAPPM
SVPHLDTRYV GGKRSLLFGP YGGFSTKYLK TGSYLDLPGS IRPNNIIPML AVGKDNLDLV
KYLVSEVTKT HAGKVEALHE YFPEADGKDW ELITAGQRVQ IIKKDAKKGG VLQFGTEVIT
AADGTLSALL GASPGASTAV PIMLELLQRC FPRKFKLEWQ DSLREMMPTY GTKLNENADL
FEQTLASTAA TLQLKTD
//
