ID N0B6H3_9BACI Unreviewed; 510 AA.
AC N0B6H3;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
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=B1NLA3E_22015 {ECO:0000313|EMBL:AGK56141.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK56141.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK56141.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK56141.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
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; CP005586; AGK56141.1; -; Genomic_DNA.
DR RefSeq; WP_015596180.1; NC_021171.1.
DR AlphaFoldDB; N0B6H3; -.
DR STRING; 666686.B1NLA3E_22015; -.
DR KEGG; baci:B1NLA3E_22015; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_028151_0_0_9; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000013300; 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; 3.50.50.60; 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:UP000013300};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00212}.
SQ SEQUENCE 510 AA; 56389 MW; 55445D92E5303D55 CRC64;
MSNRQTKTDV ILIGAGIMSA TLGSLLKELV PDWEITVFER LANAGEESSN EWNNAGTGHS
SLCELNYTVE QPDGSIDISK AIKVNEEYQV SKQFWSYLIN SKLINNPQDF IMPLPHMSMV
QGEQNVEFLK KRFETLSNNP LFKGMEFSDN PEKLMEWIPL IMQDRPSNEP IAATKIDSGT
DVNFGALTRM MFDHLKNNNV DIQYKHSVDN IKRTSDGSWE VKVRNVDDGS VERHTAKFVF
IGCGGGSLHL LQKSGIPEGK HIGGFPVSGV FMVCNNPEVV AQHHAKVYGK AAVGAPPMSV
PHLDTRFIDN KKSLLFGPFA GFSPKFLKTG SMFDLITSVK PNNVLTMLAA GAKEMSLTKY
LIQQVMLSKE QRMEELQEFI PNAKIEDWDL VVAGQRVQVI KDTAKGGKGT LQFGTEVITA
ADGSIAALLG ASPGASTAVF VMLELINKCF PQHIKEWEPK IKEMIPSYGV SLLKNPELLH
EIETSTARTL GLVGKEQEDS KSKNRMLVEA
//