P16243 · MAOC_MAIZE
- ProteinNADP-dependent malic enzyme, chloroplastic
- GeneMOD1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids636 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The chloroplastic ME isoform decarboxylates malate shuttled from neighboring mesophyll cells. The CO2 released is then refixed by ribulose-bisphosphate carboxylase. This pathway eliminates the photorespiratory loss of CO2 that occurs in most plants.
Catalytic activity
- (S)-malate + NADP+ = CO2 + NADPH + pyruvateThis reaction proceeds in the forward direction.
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Divalent metal cations. Prefers magnesium or manganese.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.23 mM | malate | |||||
14.9 μM | NADP |
kcat is 28.1 sec-1 with malate as substrate.
pH Dependence
Optimum pH is 7.5-8.0.
Pathway
Photosynthesis; C4 acid pathway.
Features
Showing features for active site, binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 184 | Proton donor | ||||
Sequence: Y | ||||||
Binding site | 237 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 255 | Proton acceptor | ||||
Sequence: K | ||||||
Binding site | 327 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 328 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 351 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 351 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 351 | Important for activity | ||||
Sequence: D | ||||||
Binding site | 380-396 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: LFLGAGEAGTGIAELIA | ||||||
Binding site | 492 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | malate dehydrogenase (decarboxylating) (NADP+) activity | |
Molecular Function | metal ion binding | |
Molecular Function | NAD binding | |
Molecular Function | oxaloacetate decarboxylase activity | |
Biological Process | malate metabolic process | |
Biological Process | pyruvate metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameNADP-dependent malic enzyme, chloroplastic
- EC number
- Short namesNADP-ME
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Andropogoneae > Tripsacinae > Zea
Accessions
- Primary accessionP16243
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 140 | Decreases kcat 8-fold. Decreases Km for NADP 2-fold, increases Km for malate 2-fold. | ||||
Sequence: F → I | ||||||
Mutagenesis | 237 | Decreases kcat 530-fold. Increases Km for NADP 36-fold and Km for malate 10-fold. | ||||
Sequence: R → L | ||||||
Mutagenesis | 255 | Increases Km for malate 10-fold, and Km for NADP 15-fold. Decreases kcat 200-fold. | ||||
Sequence: K → I | ||||||
Mutagenesis | 339 | No effect on kcat and Km for NADP. Increases Km for malate 2-fold. | ||||
Sequence: E → A | ||||||
Mutagenesis | 387 | Decreases kcat 48-fold. Increases Km for NADP 4-fold. Increases Km for malate 6-fold. | ||||
Sequence: A → G | ||||||
Mutagenesis | 392 | No effect on kcat. Increases Km for NADP 3.5-fold. Increases Km for malate 2.5-fold. | ||||
Sequence: A → G | ||||||
Mutagenesis | 435-436 | No effect on kcat and on Km for malate. Increases Km for NADP 9-fold. | ||||
Sequence: KK → LL | ||||||
Mutagenesis | 503 | No effect on kcat and Km for NADP. Increases Km for malate 2-fold. | ||||
Sequence: Q → E | ||||||
Mutagenesis | 544 | No effect on kcat and Km for NADP. Increases Km for malate 2-fold. | ||||
Sequence: L → F |
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-62 | Chloroplast | ||||
Sequence: MLSTRTAAVAASASPASPWKLGGRSEGGASCDGCRTYRNTLRRRAAPAKVRALPPRRVDAVA | ||||||
Chain | PRO_0000018547 | 63-636 | NADP-dependent malic enzyme, chloroplastic | |||
Sequence: MVSNAETETEKEQEEAAAASEELPVMPWATSVASGYTLLRDPHHNKGLAFTEEERDGHYLRGLLPPAVLSQELQIKKFMNTLRQYQTPLQRYIAMMNLQETDERLFYKLLIDNVVELLPFVYTPTVGEACQKYGSIFGRPQGLYVSLKDKGKVLEVLRNWPHRNIQVICVTDGERILGLGDLGCQGMGIPVGKLALYTALGGVDPSVCLPITIDVGTNNEFLLNDEFYIGLRQKRATGEEYDELIEEFMSAVKQFYGEKVLIQFEDFANHNAFDLLEKYSKSHLVFNDDIQGTASVVLAGLLAALKMVGGTLAEQTYLFLGAGEAGTGIAELIALEISKQTNAPIEECRKKVWLVDSKGLIVDSRKGSLQPFKKPWAHEHEPLKTLYDAVQSIKPTVLIGTSGVGRTFTKEIIEAMSSFNERPIIFSLSNPTSHSECTAEQAYTWSQGRSIFASGSPFAPVEYEGKTFVPGQSNNAYIFPGLGLGLVISGAVRVHEDMLLAASKALADQATQDNFEKGSIFPPFTSIRKISAHIAAAVAGKAYELGLATRLPPPSDLVKYAENCMYTPVYRNYR |
Proteomic databases
Expression
Gene expression databases
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-28 | Disordered | ||||
Sequence: MLSTRTAAVAASASPASPWKLGGRSEGG |
Sequence similarities
Belongs to the malic enzymes family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length636
- Mass (Da)69,824
- Last updated1990-08-01 v1
- ChecksumDF2D36FD4B2682EA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J05130 EMBL· GenBank· DDBJ | AAA33487.1 EMBL· GenBank· DDBJ | mRNA |