ID A0A1D8USB0_9PROT Unreviewed; 495 AA.
AC A0A1D8USB0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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 ECO:0000313|EMBL:GEL65487.1};
GN ORFNames=A0U89_04720 {ECO:0000313|EMBL:AOX16542.1}, KBA01_27730
GN {ECO:0000313|EMBL:GEL65487.1};
OS Kozakia baliensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Kozakia.
OX NCBI_TaxID=153496 {ECO:0000313|EMBL:AOX16542.1, ECO:0000313|Proteomes:UP000179145};
RN [1] {ECO:0000313|EMBL:AOX16542.1, ECO:0000313|Proteomes:UP000179145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16542.1,
RC ECO:0000313|Proteomes:UP000179145};
RX PubMed=27716345;
RA Brandt J.U., Jakob F., Behr J., Geissler A.J., Vogel R.F.;
RT "Dissection of exopolysaccharide biosynthesis in Kozakia baliensis.";
RL Microb. Cell Fact. 15:170-170(2016).
RN [2] {ECO:0000313|EMBL:AOX16542.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 14400 {ECO:0000313|EMBL:AOX16542.1};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:GEL65487.1, ECO:0000313|Proteomes:UP000321177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16664 {ECO:0000313|EMBL:GEL65487.1,
RC ECO:0000313|Proteomes:UP000321177};
RA Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT "Whole genome shotgun sequence of Kozakia baliensis NBRC 16664.";
RL Submitted (JUL-2019) 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; CP014674; AOX16542.1; -; Genomic_DNA.
DR EMBL; BJVW01000031; GEL65487.1; -; Genomic_DNA.
DR RefSeq; WP_070402290.1; NZ_CP014674.1.
DR AlphaFoldDB; A0A1D8USB0; -.
DR STRING; 153496.A0U89_04720; -.
DR KEGG; kba:A0U89_04720; -.
DR eggNOG; COG0579; Bacteria.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000179145; Chromosome.
DR Proteomes; UP000321177; 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:UP000179145};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ SEQUENCE 495 AA; 54660 MW; B46DE135BA9B5A55 CRC64;
MSFTAQDRPD VVLIGAGIMS ATFAALLRSL DPSLSVVAFE TLDACGLESS QAWNNAGTGH
AGNCELNYTP QKPDGSVDIS KALEVNNQFD LSRNFWAYCV RNGWVKDPAS FIRLCPHMSL
VWGEKDVAFL KARHKAMSSH HCFEGMEYSE DSATITKWAP LTMHGRDPSQ KVAATFYRGG
TDVDFGALTR ALFGHMEATA QITTFYRHKI TSMAREPDQR WRLTAKSQTD NSSVTVSARF
VFIGAGGAAL EMLQAADIPE ARSYAGFPVS GQWLRCDDPS IVGQHHAKVY GKAAVGSPPM
SVPHLDTRVI NGRSHLLFGP YAGFTTKFLK RGSWTDFYRS LNTKNILPTV QVAEDNFSLL
KYLVQQITQS SNKRFSSLHA FYPQAQKDEW KLSIAGQRVQ IIKPNEKNRG TLKFGTELVR
SADKSLVALL GASPGASVAA AVALQVIETC FADRLSDPTW QRRLHEIFPI YGIDLKNDAE
TLRANRQQTG EILKI
//