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Protein

Malate dehydrogenase [NADP], chloroplastic

Gene
N/A
Organism
Flaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Sitei88Activation of NADP-MDHBy similarity1
Sitei93Activation of NADP-MDHBy similarity1
Binding sitei198SubstratePROSITE-ProRule annotation1
Binding sitei204SubstratePROSITE-ProRule annotation1
Binding sitei211NADPBy similarity1
Binding sitei218NADP1 Publication1
Binding sitei237SubstratePROSITE-ProRule annotation1
Binding sitei268SubstratePROSITE-ProRule annotation1
Active sitei293Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi117 – 123NADP1 Publication7
Nucleotide bindingi235 – 237NADP1 Publication3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Names & Taxonomyi

Protein namesi
Recommended name:
Malate dehydrogenase [NADP], chloroplastic (EC:1.1.1.82)
Alternative name(s):
NADP-MDH
OrganismiFlaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis)
Taxonomic identifieri4224 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 68ChloroplastAdd BLAST68
ChainiPRO_000001864269 – 453Malate dehydrogenase [NADP], chloroplasticAdd BLAST385

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi88 ↔ 93In oxidized inactive NAD-MDH
Disulfide bondi429 ↔ 441In oxidized inactive NAD-MDH

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP46489.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni90 – 93Combined sources4
Beta strandi101 – 103Combined sources3
Beta strandi111 – 116Combined sources6
Turni117 – 119Combined sources3
Helixi121 – 131Combined sources11
Turni132 – 136Combined sources5
Beta strandi142 – 147Combined sources6
Helixi150 – 152Combined sources3
Helixi153 – 164Combined sources12
Turni165 – 167Combined sources3
Beta strandi171 – 178Combined sources8
Helixi180 – 183Combined sources4
Turni184 – 186Combined sources3
Beta strandi188 – 192Combined sources5
Helixi204 – 225Combined sources22
Beta strandi231 – 234Combined sources4
Beta strandi236 – 238Combined sources3
Helixi239 – 248Combined sources10
Helixi255 – 257Combined sources3
Beta strandi258 – 260Combined sources3
Helixi263 – 277Combined sources15
Beta strandi283 – 285Combined sources3
Beta strandi288 – 291Combined sources4
Beta strandi298 – 300Combined sources3
Helixi311 – 313Combined sources3
Helixi318 – 323Combined sources6
Helixi325 – 329Combined sources5
Helixi332 – 338Combined sources7
Helixi345 – 360Combined sources16
Beta strandi369 – 374Combined sources6
Beta strandi384 – 393Combined sources10
Beta strandi395 – 398Combined sources4
Helixi410 – 429Combined sources20
Turni430 – 435Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CIVX-ray2.80A69-453[»]
ProteinModelPortaliP46489.
SMRiP46489.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46489.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

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]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. 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.

P46489-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVVKLSPWA NYSSSKSEIK SSSSSSSSKS SLSAYVINVS SSPRLSFYNP
60 70 80 90 100
YPRRLHHQRL SSPASIRCSV TSSDQIQAPL PAKQKPECFG VFCLTYDLKA
110 120 130 140 150
EEETKSWKKI INVAVSGAAG MISNHLLFKL ASGEVFGPDQ PISLKLLGSE
160 170 180 190 200
RSFAALEGVA MELEDSLYPL LRQVSIGIDP YEIFQDAEWA LLIGAKPRGP
210 220 230 240 250
GMERADLLDI NGQIFAEQGK ALNAVASPNV KVMVVGNPCN TNALICLKNA
260 270 280 290 300
PNIPPKNFHA LTRLDENRAK CQLALKAGVF YDKVSNVTIW GNHSTTQVPD
310 320 330 340 350
FLNAKIHGIP VTEVIRDRKW LEDEFTNMVQ TRGGVLIKKW GRSSAASTAV
360 370 380 390 400
SIVDAIRSLV TPTPEGDWFS TGVYTNGNPY GIAEDIVFSM PCRSKGDGDY
410 420 430 440 450
EFVKDVIFDD YLSKKIKKSE DELLAEKKCV AHLTGEGIAV CDLPEDTMLP

GEM
Length:453
Mass (Da):49,515
Last modified:November 1, 1995 - v1
Checksum:i7CD3A0F9F2A7B539
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40958 mRNA. Translation: AAA63907.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L40958 mRNA. Translation: AAA63907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CIVX-ray2.80A69-453[»]
ProteinModelPortaliP46489.
SMRiP46489.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP46489.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP46489.

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]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF56327. SSF56327. 1 hit.
TIGRFAMsiTIGR01757. Malate-DH_plant. 1 hit.
TIGR01759. MalateDH-SF1. 1 hit.
PROSITEiPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMDHP_FLABI
AccessioniPrimary (citable) accession number: P46489
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 111 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

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.