Reviewed, UniProtKB/Swiss-Prot Q7XDC8 (MDHC_ORYSJ)

Names and origin

Protein names

Recommended name:
    Malate dehydrogenase, cytoplasmic
    EC=1.1.1.37
Alternative name(s):
    PP37

Gene names

Ordered Locus Names:	Os10g0478200, LOC_Os10g33800
ORF Names:	OSJNBa0055P24.3

Organism

Oryza sativa subsp. japonica (Rice)

Taxonomic identifier

39947 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › BEP clade › Ehrhartoideae › Oryzeae › Oryza

Protein attributes

Sequence length	332 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)

Catalytic activity	(S)-malate + NAD(+) = oxaloacetate + NADH.
Subunit structure	Homodimer By similarity.
Subcellular location	CytoplasmBy similarity.
Tissue specificity	Highly expressed in young panicles and immature seeds. Weakly expressed in roots and leaves. Expressed in stem and sheath (at protein level).
Post-translational modification	Phosphorylated after gibberellin treatment.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.
Sequence caution	The sequence ABG66141.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: InterPro binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 332	331	Malate dehydrogenase, cytoplasmic		PRO_0000113418
Regions
	Nucleotide binding	12 – 18	7	NAD By similarity
	Nucleotide binding	130 – 132	3	NAD By similarity
Sites
	Active site	188	1	Proton acceptor By similarity
	Binding site	93	1	Substrate carboxyl By similarity
	Binding site	99	1	Substrate carboxyl By similarity
	Binding site	106	1	NAD By similarity
	Binding site	113	1	NAD By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	163	1	Substrate carboxyl By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7XDC8-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: EB1E3187DCC4DF42	FASTA	332	35,569
	10 20 30 40 50 60 MAKEPMRVLV TGAAGQIGYA LVPMIARGVM LGADQPVILH MLDIPPATES LNGLKMELVD 70 80 90 100 110 120 AAFPLLKGIV ATTDVVEACT GVNVAVMVGG FPRKEGMERK DVMSKNVSIY KSQASALEAH 130 140 150 160 170 180 AAPNCKVLVV ANPANTNALI LKEFAPSIPE KNITCLTRLD HNRALGQISE KLNVQVTDVK 190 200 210 220 230 240 NAIIWGNHSS TQYPDVNHAT VKTPSGEKPV RELVADDEWL NTEFISTVQQ RGAAIIKARK 250 260 270 280 290 300 QSSALSAASS ACDHIRDWVL GTPEGTFVSM GVYSDGSYGV PAGLIYSFPV TCSGGEWTIV 310 320 330 QGLPIDEFSR KKMDATAQEL SEEKTLAYSC LN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, characterization and prokaryotic expression of cytosolic malate dehydrogenase from Oryza sativa." Lin C.F., Jiang R.H., Jiang L.Z., Qian X.Y., Attia K., Yang J.S. DNA Seq. 15:314-318(2004) [PubMed: 15620222] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"In-depth view of structure, activity, and evolution of rice chromosome 10." Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H. , Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R., Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A. Science 300:1566-1569(2003) [PubMed: 12791992] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Nipponbare.
[3]	"Rice proteome database based on two-dimensional polyacrylamide gel electrophoresis: its status in 2003." Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K. Nucleic Acids Res. 32:D388-D392(2004) [PubMed: 14681440] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11; 41-50; 144-153 AND 151-160, TISSUE SPECIFICITY. Strain: cv. Nipponbare. Tissue: Panicle, Sheath and Stem.
[4]	"Identification of phosphoproteins regulated by gibberellin in rice leaf sheath." Khan M.M.K., Jan A., Karibe H., Komatsu S. Plant Mol. Biol. 58:27-40(2005) [PubMed: 16028114] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, PHOSPHORYLATION. Strain: cv. Nipponbare.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF353203 mRNA. Translation: AAK26431.1. AC037425 Genomic DNA. Translation: AAG13573.1. AP008216 Genomic DNA. Translation: BAF26774.1. DP000086 Genomic DNA. Translation: AAP54283.1. DP000086 Genomic DNA. Translation: ABG66141.1. Sequence problems.
RefSeq	NP_001064860.1.
UniGene	Os.21850
3D structure databases
HSSP	HSSP built from PDB template 4MDH based on UniProtKB P11708.
ModBase	Search...
Genome annotation databases
GeneID	4348905.
KEGG	osa:4348905.
NMPDR	fig|39947.1.peg.13505.
Organism-specific databases
Gramene	Q7XDC8.
Family and domain databases
InterPro	IPR001557. L-lactate/malate_DHase. IPR001236. Lactate/malate_DHase. IPR015955. Lactate_DHase/Glyco_Ohase_4_C. IPR001252. Malate_DHase_AS. IPR011274. Malate_DHase_NAD-dep_euk. 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]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
ProDom	PD003052. Mal_dehydrog. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01759. MalateDH-SF1. 1 hit. TIGR01758. MDH_euk_cyt. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDHC_ORYSJ

Accession

Primary (citable) accession number: Q7XDC8
Secondary accession number(s): Q0IWZ1, Q109J3, Q9FWH5

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 44 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)