MQO_CLAMS
ID MQO_CLAMS Reviewed; 492 AA.
AC B0RIH2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=CMS0162;
OS Clavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / DSM 20744
OS / JCM 9667 / LMG 2889 / C-1) (Corynebacterium sepedonicum).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=31964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / C-1;
RX PubMed=18192393; DOI=10.1128/jb.01598-07;
RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J.,
RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D.,
RA Parkhill J., Ishimaru C.A.;
RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp.
RT sepedonicus suggests recent niche adaptation.";
RL J. Bacteriol. 190:2150-2160(2008).
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; AM849034; CAQ00286.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RIH2; -.
DR STRING; 31964.CMS0162; -.
DR EnsemblBacteria; CAQ00286; CAQ00286; CMS0162.
DR KEGG; cms:CMS0162; -.
DR eggNOG; COG0579; Bacteria.
DR HOGENOM; CLU_028151_0_0_11; -.
DR OMA; PHLDTRW; -.
DR UniPathway; UPA00223; UER01008.
DR Proteomes; UP000001318; 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 Gene3D; 3.50.50.60; -; 1.
DR HAMAP; MF_00212; MQO; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR006231; MQO.
DR Pfam; PF06039; Mqo; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01320; mal_quin_oxido; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..492
FT /note="Probable malate:quinone oxidoreductase"
FT /id="PRO_1000078031"
SQ SEQUENCE 492 AA; 53768 MW; 0334A61EA15E32C4 CRC64;
MSDTAESVDV VLVGGGIMSA TLGTLIKQLE PDWTIQIFER LGEVAMESSN PWNNAGTGHA
ALCELNYTPE KDGKIEIGSA TRINEQFQLS RQFWAHLVTA GAVPEPKEFI NPTPHMTFVR
GKENAEYLRR RFDALRAHPL FDAMEYTEDP AVIHSWAPLL VLQRDKDEVI AATRFEGGTD
VDFGALTNKL VDYLMEHGAA LHLNHEVRGL SKNADGTWHL RVRNDVGRST VEVDAKFVFI
GAGGGALPLL QKSGIPEIKG FGGFPISGEW FRTDDPEIVA KHRAKVYGKA AIGSPPMSVP
HLDTRVVGGE TSLLFGPYAG FSPRFLKKGS LLDLFASIRP HNIIPMLAVA KDNMSLIKYL
VSQLLASKET KFDALREFMP TADPKDWYQV TAGQRVQVMK KDAEKGGVLQ FGTEVVAAAD
GSIAGLLGAS PGASTAVPIM LDVLERCFPD CIAGWKKPLT RMIPNYGTLV ASDPKKTPKI
IRETAEVLEL QH