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B6J7Q0 (MDH_COXB1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Malate dehydrogenase

EC=1.1.1.37
Gene names
Name:mdh
Ordered Locus Names:CbuK_1102
OrganismCoxiella burnetii (strain CbuK_Q154) (Coxiella burnetii (strain Q154)) [Complete proteome] [HAMAP]
Taxonomic identifier434924 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_01517

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01517

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

malate metabolic process

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 328328Malate dehydrogenase HAMAP-Rule MF_01517
PRO_1000191619

Regions

Nucleotide binding11 – 177NAD By similarity
Nucleotide binding129 – 1313NAD By similarity

Sites

Active site1871Proton acceptor By similarity
Binding site921Substrate By similarity
Binding site981Substrate By similarity
Binding site1051NAD By similarity
Binding site1121NAD By similarity
Binding site1311Substrate By similarity
Binding site1621Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B6J7Q0 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 4A703E589E7F5F7D

FASTA32835,479
        10         20         30         40         50         60 
MAKHVKVAVT GAAGQIGYAL LFRLASGQAF GLDTTVDLHL LEIEPALPAL KGVVMELEDC 

        70         80         90        100        110        120 
AFPLLRNMVV TSDPRVAFND VNWALLVGAA PRKAGMERKD LLEKNGSIFA GQGKAINENA 

       130        140        150        160        170        180 
ASDVRIFVVG NPCNTNCLIA MNNAPDIPKD RFYAMTRLDQ NRAIGQLALK AGVDVPSVKN 

       190        200        210        220        230        240 
MIIWGNHSST QYPDFYHATI DGKPATEVIR DKNWLLNDFI PVIQQRGAAV IKARGASSAA 

       250        260        270        280        290        300 
SAANAALDSV WSLINTTPAD DNYSVALCAQ GQYGVDEGLI FSFPCRTENG VVSVIEEIEH 

       310        320 
NEFGQQKLKE TLDELREERD AVEALGLI 

« Hide

References

[1]"Comparative genomics reveal extensive transposon-mediated genomic plasticity and diversity among potential effector proteins within the genus Coxiella."
Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D., Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E., Heinzen R.A.
Infect. Immun. 77:642-656(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CbuK_Q154.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001020 Genomic DNA. Translation: ACJ20299.1.
RefSeqYP_002305444.1. NC_011528.1.

3D structure databases

ProteinModelPortalB6J7Q0.
SMRB6J7Q0. Positions 1-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING434924.CbuK_1102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ20299; ACJ20299; CbuK_1102.
GeneID7015615.
KEGGcbc:CbuK_1102.
PATRIC17917661. VBICoxBur77120_1125.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OrthoDBEOG6PP9Q2.
ProtClustDBPRK05442.

Enzyme and pathway databases

BioCycCBUR434924:GHWU-1100-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
HAMAPMF_01517. Malate_dehydrog_2.
InterProIPR001557. L-lactate/malate_DH.
IPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23382. PTHR23382. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01759. MalateDH-SF1. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_COXB1
AccessionPrimary (citable) accession number: B6J7Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: February 19, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families