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Protein

Malate:quinone oxidoreductase

Gene

mqo

Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

(S)-malate + a quinone = oxaloacetate + reduced quinone.

Cofactori

FADNote: The FAD is tightly bound.

Enzyme regulationi

Activated by lipids.

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes oxaloacetate from (S)-malate (quinone route).
Proteins known to be involved in this subpathway in this organism are:
  1. Malate:quinone oxidoreductase (mqo)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes oxaloacetate from (S)-malate (quinone route), the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Tricarboxylic acid cycle

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.1.5.4. 960.
UniPathwayiUPA00223; UER01008.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate:quinone oxidoreductase (EC:1.1.5.4)
Alternative name(s):
MQO
Malate dehydrogenase [quinone]
Gene namesi
Name:mqo
Ordered Locus Names:Cgl2001, cg2192
OrganismiCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Taxonomic identifieri196627 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium
Proteomesi
  • UP000000582 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 500499Malate:quinone oxidoreductasePRO_0000128711Add
BLAST

2D gel databases

World-2DPAGE0001:O69282.

Interactioni

Protein-protein interaction databases

STRINGi196627.cg2192.

Structurei

3D structure databases

ProteinModelPortaliO69282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the MQO family.Curated

Phylogenomic databases

eggNOGiENOG4105DWT. Bacteria.
COG0579. LUCA.
HOGENOMiHOG000109379.
KOiK00116.
OMAiEPIAATK.
OrthoDBiEOG6X6R8Z.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_00212. MQO.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR006231. MQO.
[Graphical view]
PfamiPF06039. Mqo. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01320. mal_quin_oxido. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O69282-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDSPKNAPR ITDEADVVLI GAGIMSSTLG AMLRQLEPSW TQIVFERLDG
60 70 80 90 100
PAQESSSPWN NAGTGHSALC ELNYTPEVKG KVEIAKAVGI NEKFQVSRQF
110 120 130 140 150
WSHLVEEGVL SDPKEFINPV PHVSFGQGAD QVAYIKARYE ALKDHPLFQG
160 170 180 190 200
MTYADDEATF TEKLPLMAKG RDFSDPVAIS WIDEGTDINY GAQTKQYLDA
210 220 230 240 250
AEVEGTEIRY GHEVKSIKAD GAKWIVTVKN VHTGDTKTIK ANFVFVGAGG
260 270 280 290 300
YALDLLRSAG IPQVKGFAGF PVSGLWLRCT NEELIEQHAA KVYGKASVGA
310 320 330 340 350
PPMSVPHLDT RVIEGEKGLL FGPYGGWTPK FLKEGSYLDL FKSIRPDNIP
360 370 380 390 400
SYLGVAAQEF DLTKYLVTEV LKDQDKRMDA LREYMPEAQN GDWETIVAGQ
410 420 430 440 450
RVQVIKPAGF PKFGSLEFGT TLINNSEGTI AGLLGASPGA SIAPSAMIEL
460 470 480 490 500
LERCFGDRMI EWGDKLKDMI PSYGKKLASE PALFEQQWAR TQKTLKLEEA
Length:500
Mass (Da):54,832
Last modified:January 23, 2007 - v3
Checksum:i31E02BC151758319
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224946 Genomic DNA. Translation: CAA12237.1.
BA000036 Genomic DNA. Translation: BAB99394.1.
BX927153 Genomic DNA. Translation: CAF20342.1.
RefSeqiNP_601207.1. NC_003450.3.
WP_011014814.1. NC_006958.1.

Genome annotation databases

EnsemblBacteriaiBAB99394; BAB99394; BAB99394.
CAF20342; CAF20342; cg2192.
GeneIDi1019958.
KEGGicgb:cg2192.
cgl:NCgl1926.
PATRICi21496008. VBICorGlu203724_1940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ224946 Genomic DNA. Translation: CAA12237.1.
BA000036 Genomic DNA. Translation: BAB99394.1.
BX927153 Genomic DNA. Translation: CAF20342.1.
RefSeqiNP_601207.1. NC_003450.3.
WP_011014814.1. NC_006958.1.

3D structure databases

ProteinModelPortaliO69282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi196627.cg2192.

2D gel databases

World-2DPAGE0001:O69282.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAB99394; BAB99394; BAB99394.
CAF20342; CAF20342; cg2192.
GeneIDi1019958.
KEGGicgb:cg2192.
cgl:NCgl1926.
PATRICi21496008. VBICorGlu203724_1940.

Phylogenomic databases

eggNOGiENOG4105DWT. Bacteria.
COG0579. LUCA.
HOGENOMiHOG000109379.
KOiK00116.
OMAiEPIAATK.
OrthoDBiEOG6X6R8Z.

Enzyme and pathway databases

UniPathwayiUPA00223; UER01008.
BRENDAi1.1.5.4. 960.

Family and domain databases

Gene3Di3.50.50.60. 2 hits.
HAMAPiMF_00212. MQO.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR006231. MQO.
[Graphical view]
PfamiPF06039. Mqo. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01320. mal_quin_oxido. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Biochemical and genetic characterization of the membrane-associated malate dehydrogenase (acceptor) from Corynebacterium glutamicum."
    Molenaar D., van der Rest M.E., Petrovic S.
    Eur. J. Biochem. 254:395-403(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R127.
  2. van der Rest M.E.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO N-TERMINUS.
  3. "The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
    Ikeda M., Nakagawa S.
    Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
  5. Molenaar D., van der Rest M.E., Petrovic S.
    Submitted (AUG-1998) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-6.
    Strain: R127.

Entry informationi

Entry nameiMQO_CORGL
AccessioniPrimary (citable) accession number: O69282
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 114 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.