P21528 (MDHP_PEA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Malate dehydrogenase [NADP], chloroplastic EC=1.1.1.82 Alternative name(s): NADP-MDH
Organism	Pisum sativum (Garden pea)
Taxonomic identifier	3888 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum

Protein attributes

Sequence length	441 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Plastid › chloroplast.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	malate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 58	58	Chloroplast Ref.4
	Chain	59 – 441	383	Malate dehydrogenase [NADP], chloroplastic		PRO_0000018646
Regions
	Nucleotide binding	105 – 111	7	NADP By similarity
	Nucleotide binding	223 – 225	3	NADP By similarity
Sites
	Active site	281	1	Proton acceptor By similarity
	Binding site	186	1	Substrate By similarity
	Binding site	192	1	Substrate By similarity
	Binding site	199	1	NADP By similarity
	Binding site	206	1	NAD By similarity
	Binding site	225	1	Substrate By similarity
	Binding site	256	1	Substrate By similarity
	Site	76	1	Activation of NADP-MDH
	Site	81	1	Activation of NADP-MDH
Amino acid modifications
	Disulfide bond	76 ↔ 81		In oxidized inactive NAD-MDH Ref.2
	Disulfide bond	417 ↔ 429		In oxidized inactive NAD-MDH By similarity
Experimental info
	Sequence conflict	90	1	E → T AA sequence Ref.2
	Sequence conflict	234	1	C → M AA sequence Ref.3
	Sequence conflict	287	1	P → K AA sequence Ref.3
	Sequence conflict	294	1	I → L AA sequence Ref.2
	Sequence conflict	297	1	L → I AA sequence Ref.2
	Sequence conflict	366	1	N → V AA sequence Ref.2
	Sequence conflict	377	1	S → G AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P21528 [UniParc]. Last modified February 1, 1994. Version 2. Checksum: 613747E6357C325B	FASTA	441	48,264
	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

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.
PIR	S38346.
3D structure databases
ProteinModelPortal	P21528.
SMR	P21528. Positions 71-441.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-2584130.
Proteomic databases
PRIDE	P21528.
ProMEX	P21528.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
InterPro	IPR022383. 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]
PANTHER	PTHR23382. PTHR23382. 1 hit.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMs	TIGR01757. Malate-DH_plant. 1 hit. TIGR01759. MalateDH-SF1. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDHP_PEA

Accession

Primary (citable) accession number: P21528

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	February 1, 1994
Last modified:	April 3, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program