ID A0A0D0KQT9_RHIRD Unreviewed; 561 AA.
AC A0A0D0KQT9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=RU07_13855 {ECO:0000313|EMBL:KIQ02054.1};
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358 {ECO:0000313|EMBL:KIQ02054.1, ECO:0000313|Proteomes:UP000035017};
RN [1] {ECO:0000313|EMBL:KIQ02054.1, ECO:0000313|Proteomes:UP000035017}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEJ076 {ECO:0000313|EMBL:KIQ02054.1,
RC ECO:0000313|Proteomes:UP000035017};
RA Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT draft genome assemblies.";
RL Submitted (DEC-2014) 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:KIQ02054.1}.
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DR EMBL; JXQV01000012; KIQ02054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0KQT9; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000035017; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..561
FT /note="Probable malate:quinone oxidoreductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002215273"
SQ SEQUENCE 561 AA; 61100 MW; 73135010AAEC9D22 CRC64;
MTTEFSNNDF TMNRRQVLGT AFAGLAAAAL PGAPALAQAA DKQVDVLLIG GGIMSATLGV
WLHELEPNWS IEMLERLDAV ALESSNGWNN AGTGHSALAE LNYTPETANG GIDISKAIEI
NEAFQISRQF WAWQVRNGVL KNPRSFINHT PHMSFVWGEE NIAYLEKRYE ALKASPLFAG
MQYSSDPEQI KKWVPLMMEG RDPNQKIGAT WSPLGTDMEF GEITRQFVAH LQTQKSFNLQ
TSSEVTAIER NTDGTWRVTY SNLKDDSERT VDAKFVFVGA GGGAIHLLQM SGIPEGEAYG
GFPVGGSFLV NENPDVTMLH LAKAYGKASV GSPPMSVPHL DTRVIGGKRV VLFGPFATFS
TKFLKEGSYF DLMTSTTMSN AWPMMSVGID EYPLVEYLAG QLMMSDDDRF AALQEYFPGA
KQGEWRLWQA GQRVQIIKRD AEKGGVLKLG TEIVSAKDGS IAALLGASPG ASTAAPIMLN
VLEKVFKEKV ASPEWQAKIR EIVPSYGTKL NADPEKVMQE WAYTSEHLQL PTPPQIDMAA
INAAPGAGVG EPAAQRPDMA L
//
