Reviewed, UniProtKB/Swiss-Prot P46489 (MDHP_FLABI)

Names and origin

Protein names	Recommended name:     Malate dehydrogenase [NADP], chloroplastic     EC=1.1.1.82 Alternative name(s):     NADP-MDH
Organism	Flaveria bidentis (Coastalplain yellowtops)
Taxonomic identifier	4224 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Asteroideae › Tageteae › Flaveria

Protein attributes

Sequence length	453 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.
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
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-KW
Molecular function	binding Inferred from electronic annotation. Source: InterPro malate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 68

68

Chloroplast

Chain

69 – 453

385

Malate dehydrogenase [NADP], chloroplastic

PRO_0000018642

Regions

Nucleotide binding

117 – 123

7

NADP

Nucleotide binding

235 – 237

3

NADP

Sites

Active site

293

1

Proton acceptor By similarity

Binding site

198

1

Substrate By similarity

Binding site

204

1

Substrate By similarity

Binding site

211

1

NADP By similarity

Binding site

218

1

NADP

Binding site

237

1

Substrate By similarity

Binding site

268

1

Substrate By similarity

Site

88

1

Activation of NADP-MDH By similarity

Site

93

1

Activation of NADP-MDH By similarity

Amino acid modifications

Disulfide bond

88 ↔ 93

In oxidized inactive NAD-MDH

Disulfide bond

429 ↔ 441

In oxidized inactive NAD-MDH

Secondary structure

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453

Helix Strand Turn

Details...

Turn

90 – 93

4

Beta strand

101 – 103

3

Beta strand

111 – 116

6

Turn

117 – 119

3

Helix

121 – 131

11

Turn

132 – 136

5

Beta strand

142 – 147

6

Helix

150 – 152

3

Helix

153 – 164

12

Turn

165 – 167

3

Beta strand

171 – 178

8

Helix

180 – 183

4

Turn

184 – 186

3

Beta strand

188 – 192

5

Helix

204 – 225

22

Beta strand

231 – 234

4

Beta strand

236 – 238

3

Helix

239 – 248

10

Helix

255 – 257

3

Beta strand

258 – 260

3

Helix

263 – 277

15

Beta strand

283 – 285

3

Beta strand

288 – 291

4

Beta strand

298 – 300

3

Helix

311 – 313

3

Helix

318 – 323

6

Helix

325 – 329

5

Helix

332 – 338

7

Helix

345 – 360

16

Beta strand

369 – 374

6

Beta strand

384 – 393

10

Beta strand

395 – 398

4

Helix

410 – 429

20

Turn

430 – 435

6

Sequences

	Sequence		Length	Mass (Da)
	P46489-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 7CD3A0F9F2A7B539	FASTA	453	49,515
	10 20 30 40 50 60 MAVVKLSPWA NYSSSKSEIK SSSSSSSSKS SLSAYVINVS SSPRLSFYNP YPRRLHHQRL 70 80 90 100 110 120 SSPASIRCSV TSSDQIQAPL PAKQKPECFG VFCLTYDLKA EEETKSWKKI INVAVSGAAG 130 140 150 160 170 180 MISNHLLFKL ASGEVFGPDQ PISLKLLGSE RSFAALEGVA MELEDSLYPL LRQVSIGIDP 190 200 210 220 230 240 YEIFQDAEWA LLIGAKPRGP GMERADLLDI NGQIFAEQGK ALNAVASPNV KVMVVGNPCN 250 260 270 280 290 300 TNALICLKNA PNIPPKNFHA LTRLDENRAK CQLALKAGVF YDKVSNVTIW GNHSTTQVPD 310 320 330 340 350 360 FLNAKIHGIP VTEVIRDRKW LEDEFTNMVQ TRGGVLIKKW GRSSAASTAV SIVDAIRSLV 370 380 390 400 410 420 TPTPEGDWFS TGVYTNGNPY GIAEDIVFSM PCRSKGDGDY EFVKDVIFDD YLSKKIKKSE 430 440 450 DELLAEKKCV AHLTGEGIAV CDLPEDTMLP GEM

References

[1]	Trevanion S.J., Ashton A.R. Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Leaf.
[2]	"Crystallization and preliminary crystallographic studies of chloroplast NADP-dependent malate dehydrogenase from Flaveria bidentis." Macpherson K.H., Ashton A.R., Carr P.D., Trevanion S.J., Verger D., Ollis D.L. Acta Crystallogr. D 54:654-656(1998) [PubMed: 9761865] [Abstract] Cited for: CRYSTALLIZATION.
[3]	"Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction." Carr P.D., Verger D., Ashton A.R., Ollis D.L. Structure 7:461-475(1999) [PubMed: 10196131] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT. Tissue: Leaf.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L40958 mRNA. Translation: AAA63907.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CIV	X-ray	2.80	A	69-453	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR001236. Lactate/malate_DHase.
IPR015955. Lactate_DHase/Glyco_Ohase_4_C.
IPR001252. Malate_DHase_AS.
IPR011273. Malate_DHase_NADP-dep_pln.
IPR010945. Malate_DHase_SF1.
IPR016040. NAD(P)-bd.
[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]

ProDom

PD003052. Mal_dehydrog. 1 hit.
[Graphical view] [Entries sharing at least one domain]

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

MDHP_FLABI

Accession

Primary (citable) accession number: P46489

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 25, 2008
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)