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P80541 (MDH_STEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 69. 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 attributes

Sequence length110 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

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 2 family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processmalate 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

Chain1 – ›110›110Malate dehydrogenase
PRO_0000113404

Regions

Nucleotide binding11 – 177NAD By similarity

Sites

Binding site941Substrate By similarity
Binding site1001Substrate By similarity
Binding site1071NAD By similarity

Experimental info

Non-terminal residue1101

Sequences

Sequence LengthMass (Da)Tools
P80541 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: 123924337D853F79

FASTA11011,619
        10         20         30         40         50         60 
MKAPVRVAVT GAAGQIGYAL LFRIASGEML GKDQPVILQL LELPVDKAQA ALKGVMMELE 

        70         80         90        100        110 
DCAFPLLAGM VGTDDAEVAF KDADIALLVG ARPRGPGMER KDLLLENAKI 

« Hide

References

[1]"Gene cloning, overexpression and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia."
Neumann S., Kula M.-R.
Appl. Microbiol. Biotechnol. 58:772-780(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: DSM 9181.
[2]"Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure."
Charnock C.
J. Bacteriol. 179:4066-4070(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-22.
Strain: ICPB 2648-67.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ414049 Genomic DNA. Translation: CAC93613.1.

3D structure databases

ProteinModelPortalP80541.
SMRP80541. Positions 2-110.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR001236. Lactate/malate_DH_N.
IPR010945. Malate_DH_type2.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR23382. PTHR23382. 1 hit.
PfamPF00056. Ldh_1_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDH_STEMA
AccessionPrimary (citable) accession number: P80541
Secondary accession number(s): Q8RJW4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: June 7, 2004
Last modified: February 19, 2014
This is version 69 of the entry and version 2 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