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Protein

Malate dehydrogenase [NADP], chloroplastic

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Enzyme regulationi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei76 – 761Activation of NADP-MDH
Sitei81 – 811Activation of NADP-MDH
Binding sitei186 – 1861SubstratePROSITE-ProRule annotation
Binding sitei192 – 1921SubstratePROSITE-ProRule annotation
Binding sitei199 – 1991NADPBy similarity
Binding sitei206 – 2061NADBy similarity
Binding sitei225 – 2251SubstratePROSITE-ProRule annotation
Binding sitei256 – 2561SubstratePROSITE-ProRule annotation
Active sitei281 – 2811Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi105 – 1117NADPBy similarity
Nucleotide bindingi223 – 2253NADPBy similarity

GO - Molecular functioni

  1. malate dehydrogenase (NADP+) activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. malate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase [NADP], chloroplastic (EC:1.1.1.82)
Alternative name(s):
NADP-MDH
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5858Chloroplast1 PublicationAdd
BLAST
Chaini59 – 441383Malate dehydrogenase [NADP], chloroplasticPRO_0000018646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi76 ↔ 81In oxidized inactive NAD-MDH1 Publication
Disulfide bondi417 ↔ 429In oxidized inactive NAD-MDHBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP21528.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiP21528. 1 interaction.
MINTiMINT-2584130.

Structurei

3D structure databases

ProteinModelPortaliP21528.
SMRiP21528. Positions 71-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR022383. 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]
PANTHERiPTHR23382. PTHR23382. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01757. Malate-DH_plant. 1 hit.
TIGR01759. MalateDH-SF1. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P21528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALTQLNSTC SKPQLHSSSQ LSFLSRTRTR TLPRHYHSTF APLHRTQHAR
60 70 80 90 100
ISCSVAPNQV QVPAAQTQDP KGKPDCYGVF CLTYDLKAEE ETKSWKKLIN
110 120 130 140 150
IAVSGAAGMI SNHLLFKLAS GEVFGPDQPI ALKLLGSERS IQALEGVAME
160 170 180 190 200
LEDSLFPLLR EVVISIDPYE VFQDAEWALL IGAKPRGPGV ERAALLDING
210 220 230 240 250
QIFAEQGKAL NAVASRNAKV IVVGNPCNTN ALICLKNAPN IPAKNFHALT
260 270 280 290 300
RLDENRAKCQ LALKAGVFYD KVSNMTIWGN HSTTQVPDFL NARIDGLPVK
310 320 330 340 350
EVIKDNKWLE EEFTEKVQKR GGVLIQKWGR SSAASTSVSI VDAIRSLITP
360 370 380 390 400
TPEGDWFSSG VYTNGNPYGI AEDIVFSMPC RSKGDGDYEL VNDVIFDDYL
410 420 430 440
RQKLAKTEAE LLAEKKCVAH LTGEGIAVCD LPGDTMLPGE M
Length:441
Mass (Da):48,264
Last modified:February 1, 1994 - v2
Checksum:i613747E6357C325B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti90 – 901E → T AA sequence (PubMed:1986782).Curated
Sequence conflicti234 – 2341C → M AA sequence (PubMed:3665938).Curated
Sequence conflicti287 – 2871P → K AA sequence (PubMed:3665938).Curated
Sequence conflicti294 – 2941I → L AA sequence (PubMed:1986782).Curated
Sequence conflicti297 – 2971L → I AA sequence (PubMed:1986782).Curated
Sequence conflicti366 – 3661N → V AA sequence (PubMed:1986782).Curated
Sequence conflicti377 – 3771S → G AA sequence (PubMed:1986782).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74507 mRNA. Translation: CAA52614.1.
PIRiS38346.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74507 mRNA. Translation: CAA52614.1.
PIRiS38346.

3D structure databases

ProteinModelPortaliP21528.
SMRiP21528. Positions 71-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP21528. 1 interaction.
MINTiMINT-2584130.

Proteomic databases

PRIDEiP21528.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProiIPR022383. 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]
PANTHERiPTHR23382. PTHR23382. 1 hit.
PfamiPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
SUPFAMiSSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01757. Malate-DH_plant. 1 hit.
TIGR01759. MalateDH-SF1. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiMDHP_PEA
AccessioniPrimary (citable) accession number: P21528
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: February 1, 1994
Last modified: January 7, 2015
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.