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Database: UniProt
Entry: A0A0N9VFA3_9GAMM
LinkDB: A0A0N9VFA3_9GAMM
Original site: A0A0N9VFA3_9GAMM 
ID   A0A0N9VFA3_9GAMM        Unreviewed;       546 AA.
AC   A0A0N9VFA3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=AOY20_10745 {ECO:0000313|EMBL:ALH95968.1};
OS   Acinetobacter equi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1324350 {ECO:0000313|EMBL:ALH95968.1, ECO:0000313|Proteomes:UP000064939};
RN   [1] {ECO:0000313|EMBL:ALH95968.1, ECO:0000313|Proteomes:UP000064939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114 {ECO:0000313|EMBL:ALH95968.1,
RC   ECO:0000313|Proteomes:UP000064939};
RX   PubMed=26620413;
RA   Poppel M.T., Skiebe E., Laue M., Bergmann H., Ebersberger I., Garn T.,
RA   Fruth A., Baumgardt S., Busse H.J., Wilharm G.;
RT   "Acinetobacter equi sp. nov. isolated from horse faeces.";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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; CP012808; ALH95968.1; -; Genomic_DNA.
DR   RefSeq; WP_054581856.1; NZ_CP012808.1.
DR   AlphaFoldDB; A0A0N9VFA3; -.
DR   STRING; 1324350.AOY20_10745; -.
DR   KEGG; aei:AOY20_10745; -.
DR   OrthoDB; 9763983at2; -.
DR   UniPathway; UPA00223; UER01008.
DR   Proteomes; UP000064939; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00212}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   546 AA;  61719 MW;  B465BB08405D5F5C CRC64;
     MKKVFKWVLI SLCISILLGY IFLFRPIASS INITQQKNTP TIDVVLIGGG IMSATLGTYL
     YELEPNWKVQ MFERLDQVAE ESSKGLNNAG TGHSGFMEMN YTPEKNNQIN IQKAVTTAEQ
     FEVSKQFWAY QVKHHILHNP KSFIHPVPHV AFVWGKQNVD FLKKRYASMT QNPLFYGMKY
     TENPIEIEKW APLIMHGRNL KEKVAATHMD VGSDINYGEI TKQLIQHLTT NPNFHLNTST
     EVTGISQNND KTWTISYLNL KNNQKGYIRT KYVFIGAGGA TIKLLQYTGL KEAKQYAGFP
     IGGTFLITDN PTITAQHTAK VYGRAELGAP PMSVPHIDTR YIDGKKYVLF GPFATYSNKF
     LKHGSQSDLL MATHQNNIIP MLSVGFKNLD LVQYLIDQVM MSKQEQLKEL RKYYPEAKSK
     DWNLSQGGQR VQIIKKDSDQ PAVLKFGTEI FASPDGTLTA LLGASPGAST SSYIMLTLLE
     QVFPKQVSST WNHKIKKIVP SYQQELSKDP ILLDHIRTYT SSTLGLDYTS RTTHNKDHQP
     ILNTIH
//
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