Reviewed, UniProtKB/Swiss-Prot P17606 (MDHP1_SORBI)

Names and origin

Protein names	Recommended name:     Malate dehydrogenase [NADP] 1, chloroplastic     EC=1.1.1.82 Alternative name(s):     NADP-MDH-1
Organism	Sorghum bicolor (Sorghum) (Sorghum vulgare)
Taxonomic identifier	4558 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACCAD clade › Panicoideae › Andropogoneae › Sorghum

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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, disulfides 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	Plastid › chloroplast.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 40

40

Chloroplast By similarity

Chain

41 – 429

389

Malate dehydrogenase [NADP] 1, chloroplastic

PRO_0000018647

Regions

Nucleotide binding

93 – 99

7

NADP By similarity

Nucleotide binding

211 – 213

3

NADP By similarity

Sites

Active site

269

1

Proton acceptor By similarity

Binding site

174

1

Substrate By similarity

Binding site

180

1

Substrate By similarity

Binding site

187

1

NADP By similarity

Binding site

194

1

NADP By similarity

Binding site

213

1

Substrate By similarity

Binding site

244

1

Substrate By similarity

Site

64

1

Activation of NADP-MDH

Site

69

1

Activation of NADP-MDH

Amino acid modifications

Disulfide bond

64 ↔ 69

In oxidized inactive NAD-MDH

Disulfide bond

405 ↔ 417

In oxidized inactive NAD-MDH

Experimental info

Sequence conflict

226 – 228

3

APD → PPH in CAA37531. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

429

Helix Strand Turn

Details...

Helix

66 – 68

3

Beta strand

87 – 92

6

Turn

93 – 95

3

Helix

97 – 107

11

Turn

108 – 112

5

Beta strand

118 – 123

6

Helix

126 – 128

3

Helix

129 – 140

12

Beta strand

147 – 154

8

Helix

156 – 159

4

Turn

160 – 162

3

Beta strand

164 – 168

5

Helix

180 – 201

22

Beta strand

207 – 210

4

Beta strand

212 – 214

3

Helix

215 – 224

10

Helix

231 – 233

3

Beta strand

234 – 236

3

Helix

239 – 252

14

Helix

257 – 259

3

Beta strand

264 – 267

4

Beta strand

274 – 276

3

Helix

287 – 289

3

Helix

294 – 306

13

Helix

308 – 315

8

Helix

321 – 336

16

Beta strand

345 – 350

6

Beta strand

360 – 369

10

Beta strand

372 – 374

3

Helix

386 – 405

20

Helix

407 – 410

4

Beta strand

412 – 414

3

Sequences

	Sequence		Length	Mass (Da)
	P17606-1 [UniParc]. Last modified August 1, 1990. Version 1. Checksum: 17D9E0A34A67F1FF	FASTA	429	46,455
	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

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: 2373367] [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: 2209586] [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: 10194350] [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.

PIR

JH0151.
S13588.

RefSeq

XP_002445670.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
7MDH	X-ray	2.40	A/B/C/D	55-429	[»]

ModBase

Search...

Genome annotation databases

GeneID

8057802.

KEGG

sbi:SORBI_07g023920.

Organism-specific databases

Gramene

P17606.

Phylogenomic databases

OMA

RAKCQLA.

Enzyme and pathway databases

BRENDA

1.1.1.82. 1396.

Family and domain databases

InterPro

IPR001236. Lactate/malate_DH.
IPR015955. Lactate_DH/Glyco_Ohase_4_C.
IPR001252. Malate_DH_AS.
IPR011273. Malate_DH_NADP-dep_pln.
IPR010945. Malate_DH_SF1.
IPR016040. NAD(P)-bd_dom.
[Graphical view]

Gene3D

G3DSA:3.90.110.10. lact_mal_DH. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

PANTHER

PTHR23382. MDH_SF1. 1 hit.

Pfam

PF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01757. Malate-DH_plant. 1 hit.
TIGR01759. MalateDH-SF1. 1 hit.

PROSITE

PS00068. MDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

MDHP1_SORBI

Accession

Primary (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:	February 9, 2010
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)