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Entry: A0A0S9CV85_9MICC
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ID   A0A0S9CV85_9MICC        Unreviewed;       494 AA.
AC   A0A0S9CV85;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=ASF21_14280 {ECO:0000313|EMBL:KQN97557.1};
OS   Arthrobacter sp. Leaf234.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1736303 {ECO:0000313|EMBL:KQN97557.1, ECO:0000313|Proteomes:UP000053418};
RN   [1] {ECO:0000313|Proteomes:UP000053418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000053418}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf234 {ECO:0000313|Proteomes:UP000053418};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQN97557.1}.
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DR   EMBL; LMLU01000009; KQN97557.1; -; Genomic_DNA.
DR   RefSeq; WP_055773179.1; NZ_LMLU01000009.1.
DR   AlphaFoldDB; A0A0S9CV85; -.
DR   STRING; 1736303.ASF21_14280; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000053418; 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}; Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
SQ   SEQUENCE   494 AA;  53189 MW;  2DA71D7DAE24E436 CRC64;
     MNQGTPAKTT DVVLIGGGIM SATLGAFLRQ LQPDWDVSLF ERLDVAGLES SDPWNNAGTG
     HSALCELNYS PAGKDGSVDP AKAIAINEQF QTSRQFWSHM VTEGHIGDPR SFVNAVPHMS
     FVWGQANAEY LRKRYEALSP QPLFDTMEFS EDHATIAGWT PLIMKGRNPS QPVAASRVAG
     GTDVDFGSLT RQLNAYLEGT GVGLHYSFDV LDVARASDGR WDVKVKNRAT GEATTVTSKF
     VFIGAGGGSL HLLQRTGIPE GRGFAGFPVS GQFLRCTDPT LVDQHNAKVY GQASVGAPPM
     SVPHLDTRYV KGERSLLFGP YAGFSTKFLK RGSYLDLPTS IRPSNLVPML AVAKDNMSLT
     KYLVTEVLKN RDAKNEALND FLPSADGGDW ELISAGQRVQ VIKKAPKKGG VLQFGTEVIT
     SSDGSIGALL GASPGASTAA PIMVELLKRC FPVKMSDWEP KLKEMLPGYG VKLNENPSLA
     AEIQTLTDRA LKLV
//
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