P15719

SS
Gene name
Protein name
Malate dehydrogenase [NADP], chloroplastic
Names
EC 1.1.1.82 , NADP-MDH
Species
Zea mays (Maize)
KEGG Pathway
EC number
1.1.1.82: With NAD(+) or NADP(+) as acceptor
Protein Class

Descriptions

The chloroplastic NADP-dependent malate dehydrogenase (NADP-MDH) catalyzes the reduction of oxaloacetate into L-malate. The enzyme exhibits extensions at both the N- and C-termini. The N-terminal disulfide motif is inserted in a cleft between the two subunits of the dimer, thereby locking the domains in each subunit. The C-terminal extension (C-terminal inhibitory peptide) also contains a regulatory disulfide bridge. The C-terminal disulfide keeps the C-terminal residues tight to the enzyme surface and blocks access to the active site. Reduction of the N-terminal disulfide may release the stopper between the domains and give the enzyme the flexibility. Simultaneous reduction of the C-terminal disulfide may free the C-terminal residues from binding to the enzyme and make the active site accessible.

Autoinhibitory domains (AIDs)

408-432 (C-terminal inhibitory peptide) SS

Target domain

84-412 (MDH domain)

Relief mechanism

Others

Assay

1-75 (N-terminal extension) SS

Target domain

84-412 (MDH domain)

Relief mechanism

Others

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P15719

Entry ID Method Resolution Chain Position Source
AF-P15719-F1 Predicted AlphaFoldDB

No variants for P15719

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P15719

No associated diseases with P15719

3 regional properties for P15719

Type Name Position InterPro Accession
domain Lactate/malate dehydrogenase, N-terminal 91 - 238 IPR001236
active_site Malate dehydrogenase, active site 240 - 252 IPR001252
domain Lactate/malate dehydrogenase, C-terminal 241 - 411 IPR022383

Functions

Description
EC Number 1.1.1.82 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Plastid, chloroplast
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.

2 GO annotations of molecular function

Name Definition
L-malate dehydrogenase activity Catalysis of the reaction
malate dehydrogenase (NADP+) activity Catalysis of the reaction

4 GO annotations of biological process

Name Definition
malate metabolic process The chemical reactions and pathways involving malate, the anion of hydroxybutanedioic acid, a chiral hydroxydicarboxylic acid. The (+) enantiomer is an important intermediate in metabolism as a component of both the TCA cycle and the glyoxylate cycle.
NADH metabolic process The chemical reactions and pathways involving reduced nicotinamide adenine dinucleotide (NADH), a coenzyme present in most living cells and derived from the B vitamin nicotinic acid.
oxaloacetate metabolic process The chemical reactions and pathways involving oxaloacetate, the anion of oxobutanedioic acid, an important intermediate in metabolism, especially as a component of the TCA cycle.
tricarboxylic acid cycle A nearly universal metabolic pathway in which the acetyl group of acetyl coenzyme A is effectively oxidized to two CO2 and four pairs of electrons are transferred to coenzymes. The acetyl group combines with oxaloacetate to form citrate, which undergoes successive transformations to isocitrate, 2-oxoglutarate, succinyl-CoA, succinate, fumarate, malate, and oxaloacetate again, thus completing the cycle. In eukaryotes the tricarboxylic acid is confined to the mitochondria. See also glyoxylate cycle.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P37229 Malate dehydrogenase [NADP] 2, chloroplastic Sorghum bicolor (Sorghum) (Sorghum vulgare) SS
P17606 Malate dehydrogenase [NADP] 1, chloroplastic Sorghum bicolor (Sorghum) (Sorghum vulgare) EV
10 20 30 40 50 60
MGLSTVYSPA GPRLVPAPLG RCRSAQPRRP RRAPLATVRC SVDATKQAQD GVATAVATEA
70 80 90 100 110 120
PASRKECFGV FCTTYDLKAE DKTKSWRKLV NVAVSGAAGM ISNHLLFKLA SGEVFGQDQP
130 140 150 160 170 180
IALKLLGSER SFQALEGVAM ELEDSLYPLL REVSIGIDPY VVFQDVDWAL LIGAKPRGPG
190 200 210 220 230 240
MERAALLDIN GQIFADQGKA LNAVASRNDE VLVVGNPCNT NALICLKNAP NIPAKNFHAL
250 260 270 280 290 300
TRLDENRAKC QLALKAGVFY DKVSNVTIWG NHSTTQVPDF LNAKIDGRPV KEVIKDTKWL
310 320 330 340 350 360
EEEFTLTVQK RGGVLIQKWG RSSAASTAVS IVDAIRSLVT PTPEGDWFST GVYTTGNPYG
370 380 390 400 410 420
IAEDIVFSMP CRSKGDGDYE LASDVLMDDF LWERIKKSEA ELLAEKKCVA HLTGEGNAFC
430
DLPEDTMLPG EV