ID A0A150L6H4_9BACI Unreviewed; 502 AA.
AC A0A150L6H4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=B4102_0555 {ECO:0000313|EMBL:KYD07921.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD07921.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYD07921.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYD07921.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYD07921.1}.
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DR EMBL; LQYN01000039; KYD07921.1; -; Genomic_DNA.
DR RefSeq; WP_066230750.1; NZ_LQYN01000039.1.
DR AlphaFoldDB; A0A150L6H4; -.
DR STRING; 46224.B4102_0555; -.
DR PATRIC; fig|46224.3.peg.2775; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000075666; 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 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:UP000075666};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_00212}.
SQ SEQUENCE 502 AA; 55680 MW; DBEE26EF803ACD04 CRC64;
MSNRQTSTDV ILIGAGIMSA TLGTLLKELV PDWKITVFEK LESPGEESSN EWNNAGTGHS
ALCELNYTVE KPDGTLDISK AITINEQFQL SRQFWSYLVN SNLISNPQDF IMPLPHMSLV
QGEKNVSFLK KRFEALSNNP LFQGMEFSED PNKLMEWIPL IMKDRKSTEP IAATKIDSGT
DVNFGALTRM LFDHLKSKDV DIRYKHQVED IKRLDDGLWE LKVWNMETGS IERHTSKFVF
IGGGGGSLPL LQKTGIPESK HIGGFPVSGL FLVCNNQEIV EQHHAKVYGK AAVGAPPMSV
PHLDTRYIDN KKSLLFGPFA GFSPKFLKTG SNMDLILSVK PNNVFTMLAA GAKNIPLTKY
LIQQLMLSKE QRIEELREFV PNAKSEDWDI VVAGQRVQVI KDTETGGKGT LQFGTEVITG
ANGTIAALLG ASPGASTAVH VMLEIIKKCF PEYQKEWEPK IKEMIPSYGL SLVENPDLFK
EIHTSTAKAL GLNHSEKETV SN
//
