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P17606 (MDHP1_SORBI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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] 1, chloroplastic

EC=1.1.1.82
Alternative name(s):
NADP-MDH-1
OrganismSorghum bicolor (Sorghum) (Sorghum vulgare)
Taxonomic identifier4558 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeSorghum

Protein attributes

Sequence length429 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.3

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 term3D-structure
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 – 4040Chloroplast By similarity
Chain41 – 429389Malate dehydrogenase [NADP] 1, chloroplastic
PRO_0000018647

Regions

Nucleotide binding93 – 997NADP By similarity
Nucleotide binding211 – 2133NADP By similarity

Sites

Active site2691Proton acceptor By similarity
Binding site1741Substrate By similarity
Binding site1801Substrate By similarity
Binding site1871NADP By similarity
Binding site1941NADP By similarity
Binding site2131Substrate By similarity
Binding site2441Substrate By similarity
Site641Activation of NADP-MDH
Site691Activation of NADP-MDH

Amino acid modifications

Disulfide bond64 ↔ 69In oxidized inactive NAD-MDH
Disulfide bond405 ↔ 417In oxidized inactive NAD-MDH

Experimental info

Sequence conflict226 – 2283APD → PPH in CAA37531. Ref.2

Secondary structure

........................................................... 429
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17606 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: 17D9E0A34A67F1FF

FASTA42946,455
        10         20         30         40         50         60 
MGLSTAYSPV GSHLAPAPLG HRRSAQLHRP RRALLATVRC SVDAAKQVQD GVATAEAPAT 

        70         80         90        100        110        120 
RKDCFGVFCT TYDLKAEDKT KSWKKLVNIA VSGAAGMISN HLLFKLASGE VFGQDQPIAL 

       130        140        150        160        170        180 
KLLGSERSFQ ALEGVAMELE DSLYPLLREV SIGIDPYEVF EDVDWALLIG AKPRGPGMER 

       190        200        210        220        230        240 
AALLDINGQI FADQGKALNA VASKNVKVLV VGNPCNTNAL ICLKNAPDIP AKNFHALTRL 

       250        260        270        280        290        300 
DENRAKCQLA LKAGVFYDKV SNVTIWGNHS TTQVPDFLNA KIDGRPVKEV IKDTKWLEEE 

       310        320        330        340        350        360 
FTITVQKRGG ALIQKWGRSS AASTAVSIAD AIKSLVTPTP EGDWFSTGVY TTGNPYGIAE 

       370        380        390        400        410        420 
DIVFSMPCRS KGDGDYELAT DVSMDDFLWE RIKKSEAELL AEKKCVAHLT GEGNAYCDVP 


EDTMLPGEV 

« Hide

References

[1]"Structure and characterization of the Sorghum vulgare gene encoding NADP-malate dehydrogenase."
Luchetta P., Cretin C., Gadal P.
Gene 89:171-177(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. INRA 450.
Tissue: Leaf.
[2]"Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD)."
Cretin C., Luchetta P., Joly C., Decottignies P., Lepiniec L., Gadal P., Sallantin M., Huet J.-C., Pernollet J.-C.
Eur. J. Biochem. 192:299-303(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Tamaran FNK 140.
Tissue: Leaf.
[3]"Structural basis for light activation of a chloroplast enzyme: the structure of sorghum NADP-malate dehydrogenase in its oxidized form."
Johansson K., Ramaswamy S., Saarinen M., Lemaire-Chamley M., Issakidis-Bourguet E., Miginiac-Maslow M., Eklund H.
Biochemistry 38:4319-4326(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31965 Genomic DNA. Translation: AAA34047.1.
X53453 mRNA. Translation: CAA37531.1.
PIRJH0151.
S13588.
RefSeqXP_002445670.1. XM_002445625.1.
UniGeneSbi.76.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
7MDHX-ray2.40A/B/C/D55-429[»]
ProteinModelPortalP17606.
SMRP17606. Positions 61-426.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID8057802.
KEGGsbi:SORBI_07g023920.

Organism-specific databases

GrameneP17606.

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000220953.
KOK00051.
OMAFPDYRHA.

Enzyme and pathway databases

BRENDA1.1.1.82. 5768.

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...

Other

EvolutionaryTraceP17606.

Entry information

Entry nameMDHP1_SORBI
AccessionPrimary (citable) accession number: P17606
Secondary accession number(s): P19796
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: May 14, 2014
This is version 118 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references