ID MQO_PROM0 Reviewed; 498 AA.
AC A3PBD7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Probable malate:quinone oxidoreductase {ECO:0000255|HAMAP-Rule:MF_00212};
DE EC=1.1.5.4 {ECO:0000255|HAMAP-Rule:MF_00212};
DE AltName: Full=MQO {ECO:0000255|HAMAP-Rule:MF_00212};
DE AltName: Full=Malate dehydrogenase [quinone] {ECO:0000255|HAMAP-Rule:MF_00212};
GN Name=mqo {ECO:0000255|HAMAP-Rule:MF_00212}; OrderedLocusNames=P9301_04391;
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=167546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
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:0000255|HAMAP-Rule:MF_00212};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00212};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC oxaloacetate from (S)-malate (quinone route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00212}.
CC -!- SIMILARITY: Belongs to the MQO family. {ECO:0000255|HAMAP-
CC Rule:MF_00212}.
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DR EMBL; CP000576; ABO17062.1; -; Genomic_DNA.
DR RefSeq; WP_011862439.1; NC_009091.1.
DR AlphaFoldDB; A3PBD7; -.
DR STRING; 167546.P9301_04391; -.
DR KEGG; pmg:P9301_04391; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_028151_0_0_3; -.
DR OrthoDB; 9763983at2; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000001430; 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; Flavoprotein; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..498
FT /note="Probable malate:quinone oxidoreductase"
FT /id="PRO_0000325507"
SQ SEQUENCE 498 AA; 55522 MW; B9C791ADAF64BE10 CRC64;
MTSSKNPTND NSYFDAVLVG GGIMSSTLAL LISEVLPDIK FLIIEKLNAP GSESTGAFNN
AGTGHAANCE LNYTPLDEKG NLKIDKALSI NRSFETSMSL WASLYEAGKI DIKKFLKFIP
HISFVSGQDN ISFLKKRFQK MTENPEFIDM EFSSSFDEIS SWAPLITKDR NPSTQIAATR
IGRGTDINFE ALTKEYLSLV SLNKNVEIRY KTELVDLKKI DKKQWELEIS SEGRKTSIRT
GYVFLGAGGK TINYLQKSKI PEAKSYGGFP VSGKWLICEK KDLTEKHNSK VYGKADIGSP
PMSVPHLDTR WIDNKKLLLY GPFAGFTTKF LKQSSYFDLF SSIKKNNIFS MLDVGFKNND
LINYLISQSL KNHNSRVENL KNMMPSANSS DWYLKNAGQR VQIIKKTEAG GSLKFGTEIV
NSSDGSLSAL LGASPGASTA VSIMVKVLEK SVFFLNDKHN LQKKINDLIY PELSDSENNS
TFIKDIKKRN NSIFGFHP
//
