ID A0A1H4NB86_9MICO Unreviewed; 493 AA.
AC A0A1H4NB86;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN04489806_2140 {ECO:0000313|EMBL:SEB92516.1};
OS Microbacterium humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=640635 {ECO:0000313|EMBL:SEB92516.1, ECO:0000313|Proteomes:UP000199183};
RN [1] {ECO:0000313|EMBL:SEB92516.1, ECO:0000313|Proteomes:UP000199183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21799 {ECO:0000313|EMBL:SEB92516.1,
RC ECO:0000313|Proteomes:UP000199183};
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; FNRY01000001; SEB92516.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4NB86; -.
DR STRING; 640635.SAMN04489806_2140; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000199183; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199183};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ SEQUENCE 493 AA; 54580 MW; BA64F0A40891C899 CRC64;
MTSSEPVDVA LIGGGIMSAT LASLISQLEP SWKIRIFERL GEVAQESSNP WNNAGTGHSA
LCELNYMPKS KDGSLDATKA VSINEQFQVS RQYWSYLIEK GLLDEPSTFI NGTPHMTFVR
GEDNVQYLKN RTELLKKQPL FEGIEFSDDP KKINEWAPLL MQKRRKKDLP FAATYQAAGT
DVDFGSLTRQ LFDAATKSGA TLGLNEEVRD LKQLADGTWL IRYREKVGQT PGQLRARFVF
VGAGGWALKL LQKSGIPEIK GYGVFPISGQ FLRTDNPKVV AQHQAKVYSQ AAVGAPPMSV
PHLDTRVVDG QASLLFGPYA GFSPKFLKKG HWWDIITQVR PSNLIHMLAV AKDNPDLILY
LLRELMASKH KKFESLREFM PTANPKDWYL ITAGQRAQVM KKDAKKGGVL QFGTEVISSE
DGSISGLLGA SPGASTAVPI MLNILKRCFP AKQGEWEPKL KQMIPTYGET LNDKPELADD
VLDETAEALS IHR
//
