ID A0A0B5DCG7_9CORY Unreviewed; 500 AA.
AC A0A0B5DCG7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=B842_08100 {ECO:0000313|EMBL:AJE33469.1};
OS Corynebacterium humireducens NBRC 106098 = DSM 45392.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1223515 {ECO:0000313|EMBL:AJE33469.1, ECO:0000313|Proteomes:UP000031524};
RN [1] {ECO:0000313|EMBL:AJE33469.1, ECO:0000313|Proteomes:UP000031524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFC-5 {ECO:0000313|Proteomes:UP000031524};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "Complete genome sequence of Corynebacterium humireducens DSM 45392(T),
RT isolated from a wastewater-fed microbial fuel cell.";
RL Submitted (APR-2013) 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; CP005286; AJE33469.1; -; Genomic_DNA.
DR RefSeq; WP_040086087.1; NZ_CP005286.1.
DR AlphaFoldDB; A0A0B5DCG7; -.
DR STRING; 1223515.B842_08100; -.
DR KEGG; chm:B842_08100; -.
DR HOGENOM; CLU_028151_0_0_11; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000031524; 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}.
SQ SEQUENCE 500 AA; 54883 MW; D1F119BBB0D93094 CRC64;
MSTENKNAPK VTDEVDVALV GAGVMSATLG AMIRELEPSW SQMIFERLDG PAQESSSPWN
NAGTGHSALC ELNYTPEVNG KIEVAKAIGI NEKFQVSRQF WSHQIDHGVL DDPKEWINPV
AHLAFAQGDD QVDYLKRRHE ALADNILFPG MEWVEDDAKF AERLPVMSEG RDFAAEKVAY
SGTDIGTDVN FGALTEQFLT AAEASGTEIR YGHEVKNIKK DGGKWKITVK NVHTGDTSVV
KAKFVFVGAG GYALDLLRKA GVPEVSGYAG FPVSGLWLRC TNEELINQHD AKVYGKAKVG
APPMSVPHLD TRVIDGKKGL LFGPYGGWSP KFLKEGSYLD LFKSIRLDNL PSYLGVAAQE
FALTKYLITE VAKDFEKRLV DLRDYVPSAK AEDWETVVAG QRVQVIKPAR APRFGSLEFG
TALINSTDGS IAGLLGASPG ASIAPAAMLE LVERCFGDRM IQWGPKLKEM IPSYGTKLGD
DEKMFNELWD YTQKTLKLEK
//
