ID Q1I6I3_PSEE4 Unreviewed; 545 AA.
AC Q1I6I3;
DT 13-JUN-2006, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2006, sequence version 1.
DT 27-MAR-2024, entry version 109.
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-2 {ECO:0000313|EMBL:CAK16752.1};
GN Synonyms=mqo {ECO:0000256|HAMAP-Rule:MF_00212};
GN OrderedLocusNames=PSEEN4056 {ECO:0000313|EMBL:CAK16752.1};
OS Pseudomonas entomophila (strain L48).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=384676 {ECO:0000313|EMBL:CAK16752.1, ECO:0000313|Proteomes:UP000000658};
RN [1] {ECO:0000313|EMBL:CAK16752.1, ECO:0000313|Proteomes:UP000000658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L48 {ECO:0000313|EMBL:CAK16752.1,
RC ECO:0000313|Proteomes:UP000000658};
RX PubMed=16699499; DOI=10.1038/nbt1212;
RA Vodovar N., Vallenet D., Cruveiller S., Rouy Z., Barbe V., Acosta C.,
RA Cattolico L., Jubin C., Lajus A., Segurens B., Vacherie B., Wincker P.,
RA Weissenbach J., Lemaitre B., Medigue C., Boccard F.;
RT "Complete genome sequence of the entomopathogenic and metabolically
RT versatile soil bacterium Pseudomonas entomophila.";
RL Nat. Biotechnol. 24:673-679(2006).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CT573326; CAK16752.1; -; Genomic_DNA.
DR RefSeq; WP_011535124.1; NC_008027.1.
DR AlphaFoldDB; Q1I6I3; -.
DR STRING; 384676.PSEEN4056; -.
DR World-2DPAGE; 0008:Q1I6I3; -.
DR GeneID; 32807071; -.
DR KEGG; pen:PSEEN4056; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_028151_0_0_6; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000000658; Chromosome.
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 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}; Signal {ECO:0000256|SAM:SignalP};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_00212}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..545
FT /note="Probable malate:quinone oxidoreductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004190705"
SQ SEQUENCE 545 AA; 60050 MW; C753AAEE44D729A6 CRC64;
MFKKAGKTLL GLAVAASFMQ AHAADTKKVD VLLVGGGIMS STLAVWLNEL EPSWSMEMVE
RMDGVAEESS NGWNNAGTGH SALAELNYTP LDKDGKVNIT KAIEINESFQ ISRQFWAWQV
RQGVLQNPHS FINTTPHMSF VWGDDNIKFL KQRYEALQAS PLFRSMQYSE DHAQIAKWVP
LMMEGRDPNQ KLAVTWTPIG TDVNFGEITR QFVGHLKTKE NFDLKLSSEV QDITRNEDGS
WHVEYKNLKD GTESATDAKF LFIGAGGGAL KLLQKSGIPE AKEYAGFPVG GSFLVTENPT
VAMQHMAKAY GIASTGAPPM SVPHLDTRVL DGKRVILFGP FATFSTKFLK NGSYLDLLSS
TTTHNMWPMA RVGIDQYPLV EYLAGQLMQS DDDRFAALQT YFPNAKKEDW KLWQAGQRVQ
IIKRDEEKGG VLKLGTEVVA SQDRTIAGLL GASPGASTAA PIMLNVLETV FKEKVATPEW
QAKIKEIVPS YGTKLNDSAA ATQKEWNYTA EVLQLEKPPV IDQSVGTTVV PRAPVESKPA
NDMAL
//
