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P37227 (MDHM_SCHMA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 82. 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, mitochondrial

EC=1.1.1.37
OrganismSchistosoma mansoni (Blood fluke)
Taxonomic identifier6183 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length142 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix.

Developmental stage

Expressed in relatively high level in adults as compared to larval worms.

Sequence similarities

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

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   Cellular componentMitochondrion
   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

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – ›142›142Malate dehydrogenase, mitochondrial
PRO_0000113340

Regions

Nucleotide binding1 – 66NAD By similarity
Nucleotide binding109 – 1113NAD By similarity

Sites

Binding site261NAD By similarity
Binding site731Substrate By similarity
Binding site791Substrate By similarity
Binding site861NAD By similarity
Binding site1111Substrate By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1421

Sequences

Sequence LengthMass (Da)Tools
P37227 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: C06BC6726566AE72

FASTA14214,956
        10         20         30         40         50         60 
ASGGIGEPLS LLLKQSPLIS QLALYDIAHV KGVAADLSHI ETQAHVTAHL GPGELAECLT 

        70         80         90        100        110        120 
GANVVIIPAG LPRKPGMTRD DLFNTNASIV AELIDSCAKN CPKAMICIIT NPVNSTVPIA 

       130        140 
AEILKRHNVY DPKRLFGVTT LD 

« Hide

References

[1]"Expression of Schistosoma mansoni genes involved in anaerobic and oxidative glucose metabolism during the cercaria to adult transformation."
Skelly P.J., Stein L.D., Shoemaker C.B.
Mol. Biochem. Parasitol. 60:93-104(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10108 Genomic DNA. Translation: AAA29901.1.

3D structure databases

ProteinModelPortalP37227.
SMRP37227. Positions 1-142.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP37227.

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 nameMDHM_SCHMA
AccessionPrimary (citable) accession number: P37227
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families