Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P21528 (MDHP_PEA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 107. 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 [NADP], chloroplastic

EC=1.1.1.82
Alternative name(s):
NADP-MDH
OrganismPisum sativum (Garden pea)
Taxonomic identifier3888 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Protein attributes

Sequence length441 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells.

Catalytic activity

(S)-malate + NADP+ = oxaloacetate + NADPH.

Enzyme regulation

Chloroplast NADP-MDH is activated upon illumination. In order to be enzymatically active, disulfide bridges on the protein must be reduced by thioredoxin which receives electrons from ferredoxin and the electron transport system of photosynthesis.

Subunit structure

Homodimer. Ref.4

Subcellular location

Plastidchloroplast.

Sequence similarities

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

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandNADP
   Molecular functionOxidoreductase
   PTMDisulfide bond
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

malate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmalate dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5858Chloroplast Ref.4
Chain59 – 441383Malate dehydrogenase [NADP], chloroplastic
PRO_0000018646

Regions

Nucleotide binding105 – 1117NADP By similarity
Nucleotide binding223 – 2253NADP By similarity

Sites

Active site2811Proton acceptor By similarity
Binding site1861Substrate By similarity
Binding site1921Substrate By similarity
Binding site1991NADP By similarity
Binding site2061NAD By similarity
Binding site2251Substrate By similarity
Binding site2561Substrate By similarity
Site761Activation of NADP-MDH
Site811Activation of NADP-MDH

Amino acid modifications

Disulfide bond76 ↔ 81In oxidized inactive NAD-MDH Ref.2
Disulfide bond417 ↔ 429In oxidized inactive NAD-MDH By similarity

Experimental info

Sequence conflict901E → T AA sequence Ref.2
Sequence conflict2341C → M AA sequence Ref.3
Sequence conflict2871P → K AA sequence Ref.3
Sequence conflict2941I → L AA sequence Ref.2
Sequence conflict2971L → I AA sequence Ref.2
Sequence conflict3661N → V AA sequence Ref.2
Sequence conflict3771S → G AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P21528 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 613747E6357C325B

FASTA44148,264
        10         20         30         40         50         60 
MALTQLNSTC SKPQLHSSSQ LSFLSRTRTR TLPRHYHSTF APLHRTQHAR ISCSVAPNQV 

        70         80         90        100        110        120 
QVPAAQTQDP KGKPDCYGVF CLTYDLKAEE ETKSWKKLIN IAVSGAAGMI SNHLLFKLAS 

       130        140        150        160        170        180 
GEVFGPDQPI ALKLLGSERS IQALEGVAME LEDSLFPLLR EVVISIDPYE VFQDAEWALL 

       190        200        210        220        230        240 
IGAKPRGPGV ERAALLDING QIFAEQGKAL NAVASRNAKV IVVGNPCNTN ALICLKNAPN 

       250        260        270        280        290        300 
IPAKNFHALT RLDENRAKCQ LALKAGVFYD KVSNMTIWGN HSTTQVPDFL NARIDGLPVK 

       310        320        330        340        350        360 
EVIKDNKWLE EEFTEKVQKR GGVLIQKWGR SSAASTSVSI VDAIRSLITP TPEGDWFSSG 

       370        380        390        400        410        420 
VYTNGNPYGI AEDIVFSMPC RSKGDGDYEL VNDVIFDDYL RQKLAKTEAE LLAEKKCVAH 

       430        440 
LTGEGIAVCD LPGDTMLPGE M 

« Hide

References

[1]"Cloning, site-specific mutagenesis, expression and characterization of full-length chloroplast NADP-malate dehydrogenase from Pisum sativum."
Reng W., Riessland R., Scheibe R., Jaenicke R.
Eur. J. Biochem. 217:189-197(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Primary structure and analysis of the location of the regulatory disulfide bond of pea chloroplast NADP-malate dehydrogenase."
Scheibe R., Kampfenkel K., Wessels R., Tripier D.
Biochim. Biophys. Acta 1076:1-8(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 65-441, DISULFIDE BOND.
Strain: cv. Kleine Rheinlaenderin.
[3]"Amino acid sequence similarity between malate dehydrogenases (NAD) and pea chloroplast malate dehydrogenase (NADP)."
Fickenscher K., Scheibe R., Marcus F.
Eur. J. Biochem. 168:653-658(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[4]"Limited proteolysis of NADP-malate dehydrogenase from pea chloroplast by aminopeptidase K yields monomers. Evidence of proteolytic degradation of NADP-malate dehydrogenase during purification from pea."
Kampfenkel K.
Biochim. Biophys. Acta 1156:71-77(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 59-74 AND 92-112, SUBUNIT.
Strain: cv. Kleine Rheinlaenderin.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X74507 mRNA. Translation: CAA52614.1.
PIRS38346.

3D structure databases

ProteinModelPortalP21528.
SMRP21528. Positions 71-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP21528. 1 interaction.
MINTMINT-2584130.

Proteomic databases

PRIDEP21528.
ProMEXP21528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR022383. Lactate/malate_DH_C.
IPR001236. Lactate/malate_DH_N.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR011273. Malate_DH_NADP-dep_pln.
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]
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01757. Malate-DH_plant. 1 hit.
TIGR01759. MalateDH-SF1. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDHP_PEA
AccessionPrimary (citable) accession number: P21528
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1994
Last modified: February 19, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families