ID A0A239EWV8_9MICO Unreviewed; 503 AA.
AC A0A239EWV8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=SAMN06309944_0495 {ECO:0000313|EMBL:SNS49250.1};
OS Micrococcales bacterium KH10.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales.
OX NCBI_TaxID=1945885 {ECO:0000313|EMBL:SNS49250.1, ECO:0000313|Proteomes:UP000198369};
RN [1] {ECO:0000313|EMBL:SNS49250.1, ECO:0000313|Proteomes:UP000198369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH10 {ECO:0000313|EMBL:SNS49250.1,
RC ECO:0000313|Proteomes:UP000198369};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZPE01000001; SNS49250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239EWV8; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000198369; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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:UP000198369};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ SEQUENCE 503 AA; 55066 MW; 3023D85D36B92502 CRC64;
MPSTVSVSTH ASAAQASSAQ PAPILFANRG SDIAGQHYDA VLVGGGIMSA TLGTFLSLLE
PTWRILIVER LDEVARESSN PWNNAGTGHA ALCELNYTPE RPDGTIETTK AATINRNFEV
SRTLWAALTR RGLIPDPSRF LSVTPHMTLV RGAKDVDYLK RRYEAIREVP GFTSMEFSTD
RDTIASWAPL LVAGRRDEPI AATRVAEGTD INFGALTREL IDILRHRGTE LRTNHEVTKL
HRRGGKWQVQ IKDRRWNASR RPAKITADFV FVGAGGYALP LLQRSGIKEI RGYGGFPISG
KFLRTTNPDI VAKHQAKVYG KASVGSPPMS VPHLDTRVVD GKEALLFGPY AGFSPRYLKT
GSLWDLVRSL RLGNIISMVG AGWHNMDLTR YLIGQLIARD ETQFRALLDF YPEAKPGDWE
WITAGQRVQV IKRDKGKGGK LEFGTELVTS SDGSIAGLLG ASPGASTAAA TMVRLLKTCF
PDRIDSWRSD LEELVPGAFD SVG
//
