ID A0A0D6TRI4_9FLAO Unreviewed; 492 AA.
AC A0A0D6TRI4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=SY27_00680 {ECO:0000313|EMBL:KIX22402.1};
OS Flavobacterium sp. 316.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1603293 {ECO:0000313|EMBL:KIX22402.1, ECO:0000313|Proteomes:UP000032747};
RN [1] {ECO:0000313|EMBL:KIX22402.1, ECO:0000313|Proteomes:UP000032747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=316 {ECO:0000313|EMBL:KIX22402.1,
RC ECO:0000313|Proteomes:UP000032747};
RA Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT Genomic and a Proteomic Perspective.";
RL Submitted (FEB-2015) 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:KIX22402.1}.
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DR EMBL; JYGZ01000001; KIX22402.1; -; Genomic_DNA.
DR RefSeq; WP_045966485.1; NZ_JYGZ01000001.1.
DR AlphaFoldDB; A0A0D6TRI4; -.
DR STRING; 1603293.SY27_00680; -.
DR PATRIC; fig|1603293.4.peg.139; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000032747; 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:UP000032747};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ SEQUENCE 492 AA; 55222 MW; A93CDC5EE3DFF6F3 CRC64;
MEEPDVILIG AGIMSATLGI LIKELEPNCK IEIYERLSEA ASESSDAWNN AGTGHAAFCE
LNYTPEKEDG TIDITKALKI SEAYEVSRQF WSYLVQKGIL KNPEIFIHSI PHISFVWGKE
NVAFLKKRHE ALTKKSLFKR MLFSDDKAVL EEWMPLVMHN RDKNEVHAAT YMPIGTDVNF
GTLTRALFEY LKDQEGVTLY FQTEVEKLKK QEDGNWKVKV RNLETHKSRK VKTPFVFIGA
GGGSLRLLEK ADIEEGNGFG GFPISGQWLR CMNPEIIKQH KAKVYGKASV GSPPMSVPHI
DTRVIDGKQE LLFGPYAGFT TKFLKNGSYL DLIKSIQTDN IRPMLSAGIN NIPLTKYLIE
QVMQSQEDRM KALRDYFPNA KSEDWVLETA GKRVQVIKKD KNGKGVLEFG TELVNDDDGS
LAVLLGASPG ASTSVSVMIE VLSKCFANQY NSEAWQNKFK EMIPAFGQTL NDNDELCTQI
RAMTSKTLKL VN
//
