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P0C1G5 (MDH_KLEPR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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
OrganismKlebsiella pneumoniae subsp. rhinoscleromatis
Taxonomic identifier39831 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

Protein attributes

Sequence length114 AA.
Sequence statusFragment.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible oxidation of malate to oxaloacetate By similarity.

Catalytic activity

(S)-malate + NAD+ = oxaloacetate + NADH.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the LDH/MDH superfamily. MDH type 1 family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionL-malate dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›114›114Malate dehydrogenase
PRO_0000240201

Regions

Nucleotide binding87 – 893NAD By similarity

Sites

Binding site41NAD By similarity
Binding site511Substrate By similarity
Binding site571Substrate By similarity
Binding site641NAD By similarity
Binding site891Substrate By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1141

Sequences

Sequence LengthMass (Da)Tools
P0C1G5 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: D63AEB7FD35062AE

FASTA11411,913
        10         20         30         40         50         60 
SLYDIAPVTP GVAVDLSHIP TDVKIKGFSG EDATPALEGA DVVLISAGVA RKPGMDRSDL 

        70         80         90        100        110 
FNVNAGIVKN LVQQIAKTRP QACIGIITNP VNTTVAIAAE VLKKAGVYDK NKLF 

« Hide

References

[1]"Diversity and evolution of the class A chromosomal beta-lactamase gene in Klebsiella pneumoniae."
Haeggman S., Loefdahl S., Paauw A., Verhoef J., Brisse S.
Antimicrob. Agents Chemother. 48:2400-2408(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13884 / JCM 1664 / LMG 3184 / NCTC 5046 / R-70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ635391 Genomic DNA. Translation: CAG25802.1.

3D structure databases

ProteinModelPortalP0C1G5.
SMRP0C1G5. Positions 1-114.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR001557. L-lactate/malate_DH.
IPR001236. Lactate/malate_DH_N.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF00056. Ldh_1_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_KLEPR
AccessionPrimary (citable) accession number: P0C1G5
Secondary accession number(s): P80535
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: February 19, 2014
This is version 36 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