ID A0A0G3GQA5_9CORY Unreviewed; 500 AA.
AC A0A0G3GQA5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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 ECO:0000313|EMBL:AKK03391.1};
GN ORFNames=CEPID_07705 {ECO:0000313|EMBL:AKK03391.1};
OS Corynebacterium epidermidicanis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1050174 {ECO:0000313|EMBL:AKK03391.1, ECO:0000313|Proteomes:UP000035368};
RN [1] {ECO:0000313|EMBL:AKK03391.1, ECO:0000313|Proteomes:UP000035368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45586 {ECO:0000313|EMBL:AKK03391.1,
RC ECO:0000313|Proteomes:UP000035368};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium epidermidicanis DSM 45586,
RT isolated from the skin of a dog suffering from pruritus.";
RL Submitted (MAY-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; CP011541; AKK03391.1; -; Genomic_DNA.
DR RefSeq; WP_047240435.1; NZ_CP011541.1.
DR AlphaFoldDB; A0A0G3GQA5; -.
DR STRING; 1050174.CEPID_07705; -.
DR KEGG; cei:CEPID_07705; -.
DR PATRIC; fig|1050174.4.peg.1551; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000035368; 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:UP000035368};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ SEQUENCE 500 AA; 54724 MW; CE2E6C566B7B5E4F CRC64;
MSDAKVKAQS VTEEADVVLV GAGIMSATLG AMLRQLEPQW SQVVFERLDV PAAESSSPWN
NAGTGHSALC ELNYTPLRDG QVDISKAISI NEKFQVSRQF WAHQVEHGVL TNPEEFIQPV
PHVSFGRGDE QVNYIQMRYE KLSKHPLFPG MQFSDDEAKF AEFLPLMAKG RDFDAEKVAI
SWFESGTDIN YGAQARQFLN AAEKGGTEVK YGHEVKDIKK DGAKWKVVVK NVHTGDLQTY
RAKFVFVGAG GMALPLLQKS GIAEVKGFGG FPVSGAWLRC TNDELIGQHA AKVYGQASVG
TPPMSVPHLD TRVIDGKKGL LFGPYAGWTP KFLKQGSMLD LFKSIRVGNI PSYLGVAAQE
MGLTKYLVTE VLKDEGARLE ALRSYMPTAK AEDWELVIAG QRVQVIKPTA APRFGSLEFG
TALINNPEGT IAGLLGASPG ASIAPAAMIE VLERCFGHRM IEWGPKLKEM VPSYGQKLAV
NPGLFDEVWN HTQKTLKLEK
//
