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C1CY73 (MDH_DEIDV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 38. 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:Deide_20240
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length330 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 – 330330Malate dehydrogenase HAMAP-Rule MF_01517
PRO_1000215355

Regions

Nucleotide binding13 – 197NAD By similarity
Nucleotide binding131 – 1333NAD By similarity

Sites

Active site1891Proton acceptor By similarity
Binding site941Substrate By similarity
Binding site1001Substrate By similarity
Binding site1071NAD By similarity
Binding site1141NAD By similarity
Binding site1331Substrate By similarity
Binding site1641Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
C1CY73 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: D082DAEA0E614880

FASTA33035,298
        10         20         30         40         50         60 
MTNKQPVRVA VTGAAGQIGY SLLFRIAAGD MLGKDQPVIL QLLEITPALK ALQGVVMELR 

        70         80         90        100        110        120 
DGAYPLLADV VTSDDPLVAF KDADYALLVG AMPRKAGMER GDLLGANGGI FKPQGQALNQ 

       130        140        150        160        170        180 
VASRDVKVLV VGNPANTNAL IAQQNAPDLD PRQFTAMVRL DHNRAISQLA EKTGQPVSAI 

       190        200        210        220        230        240 
KNITIWGNHS STQYPDLSQA TVGGRPALDL VDRTWYEQEY IPTVAKRGAA IIEARGASSA 

       250        260        270        280        290        300 
ASAASAAIDH MRDWALGTSE GEWVSMGIPS DGSYGVPEGL IYGFPVTVKD GKYQIVQGLE 

       310        320        330 
ISEFSRGKMD ATARELEEER DEIRKLGLIS 

« Hide

References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001114 Genomic DNA. Translation: ACO47029.1.
RefSeqYP_002786783.1. NC_012526.1.

3D structure databases

ProteinModelPortalC1CY73.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING546414.Deide_20240.

Proteomic databases

PaxDbC1CY73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO47029; ACO47029; Deide_20240.
GeneID7737744.
KEGGddr:Deide_20240.
PATRIC21618096. VBIDeiDes121019_2321.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00024.
OMAWLENIMI.
OrthoDBEOG6PP9Q2.

Enzyme and pathway databases

BioCycDDES546414:GHOM-2289-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.
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.
ProtoNetSearch...

Entry information

Entry nameMDH_DEIDV
AccessionPrimary (citable) accession number: C1CY73
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: May 14, 2014
This is version 38 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