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P15719

- MDHP_MAIZE

UniProt

P15719 - MDHP_MAIZE

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Protein

Malate dehydrogenase [NADP], chloroplastic

Gene
N/A
Organism
Zea mays (Maize)
Status
Reviewed - 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
Sitei67 – 671Activation of NADP-MDH
Sitei72 – 721Activation of NADP-MDH
Binding sitei177 – 1771SubstratePROSITE-ProRule annotation
Binding sitei183 – 1831SubstratePROSITE-ProRule annotation
Binding sitei190 – 1901NADPBy similarity
Binding sitei197 – 1971NADBy similarity
Binding sitei216 – 2161SubstratePROSITE-ProRule annotation
Binding sitei247 – 2471SubstratePROSITE-ProRule annotation
Active sitei272 – 2721Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi96 – 1027NADPBy similarity
Nucleotide bindingi214 – 2163NADPBy similarity

GO - Molecular functioni

  1. L-malate dehydrogenase activity Source: EnsemblPlants/Gramene
  2. malate dehydrogenase (NADP+) activity Source: UniProtKB-EC

GO - Biological processi

  1. glucosinolate biosynthetic process Source: EnsemblPlants/Gramene
  2. malate metabolic process Source: EnsemblPlants/Gramene
  3. maltose metabolic process Source: EnsemblPlants/Gramene
  4. photosystem II assembly Source: EnsemblPlants/Gramene
  5. plastid organization Source: EnsemblPlants/Gramene
  6. positive regulation of catalytic activity Source: EnsemblPlants/Gramene
  7. rRNA processing Source: EnsemblPlants/Gramene
  8. starch biosynthetic process Source: EnsemblPlants/Gramene
  9. tricarboxylic acid cycle Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.1.1.82. 6752.

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase [NADP], chloroplastic (EC:1.1.1.82)
Alternative name(s):
NADP-MDH
OrganismiZea mays (Maize)
Taxonomic identifieri4577 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Organism-specific databases

GrameneiP15719.
MaizeGDBi40092.

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: EnsemblPlants/Gramene
  2. chloroplast envelope Source: EnsemblPlants/Gramene
  3. chloroplast stroma Source: EnsemblPlants/Gramene
  4. mitochondrion Source: EnsemblPlants/Gramene
  5. thylakoid Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4040Chloroplast1 PublicationAdd
BLAST
Chaini41 – 432392Malate dehydrogenase [NADP], chloroplasticPRO_0000018643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi67 ↔ 72In oxidized inactive NAD-MDH1 Publication
Disulfide bondi408 ↔ 420In oxidized inactive NAD-MDHBy similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP15719.

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP15719.
SMRiP15719. Positions 64-429.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

HOGENOMiHOG000220953.
KOiK00051.

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.

P15719-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGLSTVYSPA GPRLVPAPLG RCRSAQPRRP RRAPLATVRC SVDATKQAQD
60 70 80 90 100
GVATAVATEA PASRKECFGV FCTTYDLKAE DKTKSWRKLV NVAVSGAAGM
110 120 130 140 150
ISNHLLFKLA SGEVFGQDQP IALKLLGSER SFQALEGVAM ELEDSLYPLL
160 170 180 190 200
REVSIGIDPY VVFQDVDWAL LIGAKPRGPG MERAALLDIN GQIFADQGKA
210 220 230 240 250
LNAVASRNDE VLVVGNPCNT NALICLKNAP NIPAKNFHAL TRLDENRAKC
260 270 280 290 300
QLALKAGVFY DKVSNVTIWG NHSTTQVPDF LNAKIDGRPV KEVIKDTKWL
310 320 330 340 350
EEEFTLTVQK RGGVLIQKWG RSSAASTAVS IVDAIRSLVT PTPEGDWFST
360 370 380 390 400
GVYTTGNPYG IAEDIVFSMP CRSKGDGDYE LASDVLMDDF LWERIKKSEA
410 420 430
ELLAEKKCVA HLTGEGNAFC DLPEDTMLPG EV
Length:432
Mass (Da):46,860
Last modified:April 1, 1990 - v1
Checksum:i45531DEF8BBF79FD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16084 mRNA. Translation: CAA34213.1.
PIRiS04859. DEMZMC.
RefSeqiNP_001105420.1. NM_001111950.1.
UniGeneiZm.122.

Genome annotation databases

GeneIDi542374.
KEGGizma:542374.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X16084 mRNA. Translation: CAA34213.1 .
PIRi S04859. DEMZMC.
RefSeqi NP_001105420.1. NM_001111950.1.
UniGenei Zm.122.

3D structure databases

ProteinModelPortali P15719.
SMRi P15719. Positions 64-429.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P15719.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 542374.
KEGGi zma:542374.

Organism-specific databases

Gramenei P15719.
MaizeGDBi 40092.

Phylogenomic databases

HOGENOMi HOG000220953.
KOi K00051.

Enzyme and pathway databases

BRENDAi 1.1.1.82. 6752.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR23382. PTHR23382. 1 hit.
Pfami PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56327. SSF56327. 1 hit.
TIGRFAMsi TIGR01757. Malate-DH_plant. 1 hit.
TIGR01759. MalateDH-SF1. 1 hit.
PROSITEi PS00068. MDH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Maize NADP-malate dehydrogenase: cDNA cloning, sequence, and mRNA characterization."
    Metzler M., Rothermel B.A., Nelson T.
    Plant Mol. Biol. 12:713-722(1989)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leaf.
  2. "Primary structure of the light-dependent regulatory site of corn NADP-malate dehydrogenase."
    Decottignies P., Schmitter J.-M., Miginiac-Maslow M., le Marechal P., Jacquot J.-P., Gadal P.
    J. Biol. Chem. 263:11780-11785(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 58-84.
  3. "Amino acid sequence and molecular weight of native NADP malate dehydrogenase from the C4 plant Zea mays."
    Agostino A., Jeffrey P., Hatch M.D.
    Plant Physiol. 98:1506-1510(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 41-62.

Entry informationi

Entry nameiMDHP_MAIZE
AccessioniPrimary (citable) accession number: P15719
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 119 of the entry and version 1 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