ID A0A1G7HB61_9ACTN Unreviewed; 500 AA.
AC A0A1G7HB61;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=SAMN05660662_0493 {ECO:0000313|EMBL:SDE97682.1};
OS Blastococcus aurantiacus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1550231 {ECO:0000313|EMBL:SDE97682.1, ECO:0000313|Proteomes:UP000199406};
RN [1] {ECO:0000313|EMBL:SDE97682.1, ECO:0000313|Proteomes:UP000199406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44268 {ECO:0000313|EMBL:SDE97682.1,
RC ECO:0000313|Proteomes:UP000199406};
RA de Groot N.N.;
RL Submitted (OCT-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; FNBT01000001; SDE97682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7HB61; -.
DR STRING; 1550231.SAMN05660662_0493; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000199406; Unassembled WGS sequence.
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; 53908 MW; 31894FB69625F296 CRC64;
MTSDHGVVAD SANPDVVLVG GGIMSATLAA LFGIVAPDWS VTVFEAGPAL AGESSDAWNN
AGTGHSALCE LNYTPAGPDG RVDASKAVGI NEQFQVSRQF WSHLVRRGMT ASPRDFISPV
PHVSFVTGDE GRRYMRNRYS ALKAEPLFGE LEHTEDPAEL ARWIPLVMAG RDPEQAVAAT
RSIAGTDVNF GALTKLLLAD AENRGVAAHT HQRVEEIERE TDGRWKVTVR DTRSGEPRTV
RARFVFVGAG GGALPLLQRT GIPEIAGFGG FPVSGMFLRT TSQELVRMHQ AKVYGQAAVG
APPMSVPHLD LRLIDGEHSL LFGPYAGFSP KFLKAGSMFD LPLSVRPNNL GSMLGVARTE
LALTKYLIKE LLQSRAARHR TLQGFVPEAE EHDWDMITAG QRVQVIKRDP STSKGMLQFG
TELIVGADGT IAGLLGASPG ASTAVAAMLT LLERCFPDRT QAWRPLIQEA IPSYGHKLSE
EPELLAQVRK DTMETLELDG
//