Reviewed, UniProtKB/Swiss-Prot O48902 (MDHP_MEDSA)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase [NADP], chloroplastic
    EC=1.1.1.82
Alternative name(s):
    NADP-MDH

Gene names

Name:	MDH1
Synonyms:	P1MDH

Organism

Medicago sativa (Alfalfa)

Taxonomic identifier

3879 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Trifolieae › Medicago

Protein attributes

Sequence length	437 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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 By similarity.
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 By similarity.
Subunit structure	Homodimer By similarity.
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
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 – 49	49	Chloroplast Potential
	Chain	50 – 437	388	Malate dehydrogenase [NADP], chloroplastic		PRO_0000018644
Regions
	Nucleotide binding	101 – 107	7	NADP By similarity
	Nucleotide binding	219 – 221	3	NADP By similarity
Sites
	Active site	277	1	Proton acceptor By similarity
	Binding site	182	1	Substrate By similarity
	Binding site	188	1	Substrate By similarity
	Binding site	195	1	NADP By similarity
	Binding site	202	1	NAD By similarity
	Binding site	221	1	Substrate By similarity
	Binding site	252	1	Substrate By similarity
	Site	72	1	Activation of NADP-MDH By similarity
	Site	77	1	Activation of NADP-MDH By similarity
Amino acid modifications
	Disulfide bond	72 ↔ 77		In oxidized inactive NAD-MDH By similarity
	Disulfide bond	413 ↔ 425		In oxidized inactive NAD-MDH By similarity

Sequences

	Sequence		Length	Mass (Da)
	O48902-1 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 9C7C5377DBA5454A	FASTA	437	47,835
	10 20 30 40 50 60 MALTQLNNTC SKTQLHSSSQ LSFLSRTLPR HHHCTLAPLH RTQHARISCS VAPNQVQAPA 70 80 90 100 110 120 VQTQDPKSKP DCYGVFCLTY DLKAEEETKS WKKLITIAVS GAAGMISNHL LFKLASGEVF 130 140 150 160 170 180 GPNQPIALKL LGSERSLQAL EGVAMELEDS LFPLLREVVI SIDPYEVFQD AEWALLIGAK 190 200 210 220 230 240 PRGPGMERAA LLDINGQIFA EQGKALNAVA SRNVKVIVVG NPCNTNALIC LKNAPNIPAK 250 260 270 280 290 300 NFHALTRLDE NRAKCQLALK AGVFYDKVSN MTIWGNHSTT QVPDFLNARI DGLPVKEVIK 310 320 330 340 350 360 DHKWLEEEFT EKVQKRGGAL IQKWGRSSAA STSVSIVDAI RSLIIPTPEG DWFSTGVYTT 370 380 390 400 410 420 GNPYGIAEDI VFSMPCRSKG DGDYELVKDV IFDDYLRQKL AKTEAELLAE KKCVAHLTGE 430 GIAVCDLPGD TMLPGEM

References

[1]

"Alfalfa malate dehydrogenase (MDH): molecular cloning and characterization of five different forms reveals a unique nodule-enhanced MDH." Miller S.S., Driscoll B.T., Gregerson R.G., Gantt J.S., Vance C.P. Plant J. 15:173-184(1998) [PubMed: 9721676] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Saranac. Tissue: Root nodule.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF020269 mRNA. Translation: AAB99753.1.
3D structure databases
HSSP	HSSP built from PDB template 1CIV based on UniProtKB P46489.
SMR	O48902. Positions 69-434.
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_MEDSA

Accession

Primary (citable) accession number: O48902

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	June 1, 1998
Last modified:	November 25, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)