Q9ZP06 (MDHM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malate dehydrogenase 1, mitochondrial
EC=1.1.1.37

Alternative name(s):
mNAD-MDH 1

Gene names

Ordered Locus Names:	At1g53240
ORF Names:	F12M16.14

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	341 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	Mitochondrion matrix Ref.6 Ref.7.
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.
Sequence caution	The sequence AAF69549.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro defense response to bacterium Inferred from expression pattern. Source: TAIR malate metabolic process Inferred from electronic annotation. Source: InterPro response to cadmium ion Inferred from expression pattern. Source: TAIR response to cold Inferred from expression pattern. Source: TAIR response to salt stress Inferred from expression pattern. Source: TAIR tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cell wall Inferred from direct assay. Source: TAIR chloroplast Inferred from direct assay. Source: TAIR mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-malate dehydrogenase activity Inferred from mutant phenotype. Source: TAIR copper ion binding Inferred from direct assay. Source: TAIR nucleotide 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
	Transit peptide	1 – 22	22	Mitochondrion Ref.6
	Chain	23 – 341	319	Malate dehydrogenase 1, mitochondrial		PRO_0000018622
Regions
	Nucleotide binding	36 – 42	7	NAD By similarity
	Nucleotide binding	145 – 147	3	NAD By similarity
Sites
	Active site	205	1	Proton acceptor By similarity
	Binding site	62	1	NAD By similarity
	Binding site	109	1	Substrate By similarity
	Binding site	115	1	Substrate By similarity
	Binding site	122	1	NAD By similarity
	Binding site	147	1	Substrate By similarity
	Binding site	181	1	Substrate By similarity
	Binding site	256	1	NAD By similarity
Amino acid modifications
	Modified residue	23	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	17	1	V → A in AAM64855. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9ZP06 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: D035C4C38785BE57	FASTA	341	35,804
	10 20 30 40 50 60 MFRSMLVRSS ASAKQAVIRR SFSSGSVPER KVAILGAAGG IGQPLALLMK LNPLVSSLSL 70 80 90 100 110 120 YDIANTPGVA ADVGHINTRS EVVGYMGDDN LAKALEGADL VIIPAGVPRK PGMTRDDLFN 130 140 150 160 170 180 INAGIVKNLC TAIAKYCPHA LINMISNPVN STVPIAAEIF KKAGMYDEKK LFGVTTLDVV 190 200 210 220 230 240 RARTFYAGKA NVPVAEVNVP VIGGHAGVTI LPLFSQATPQ ANLSSDILTA LTKRTQDGGT 250 260 270 280 290 300 EVVEAKAGKG SATLSMAYAG ALFADACLKG LNGVPDVIEC SYVQSTITEL PFFASKVRLG 310 320 330 340 KNGVEEVLDL GPLSDFEKEG LEALKPELKS SIEKGVKFAN Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel, non-redox-regulated NAD-dependent malate dehydrogenase from chloroplasts of Arabidopsis thaliana L." Berkemeyer M., Scheibe R., Ocheretina O. J. Biol. Chem. 273:27927-27933(1998) [PubMed: 9774405] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Proteomic approach to identify novel mitochondrial proteins in Arabidopsis." Kruft V., Eubel H., Jaensch L., Werhahn W., Braun H.-P. Plant Physiol. 127:1694-1710(2001) [PubMed: 11743114] [Abstract] Cited for: PROTEIN SEQUENCE OF 23-37, SUBCELLULAR LOCATION. Tissue: Leaf and Stem.
[7]	"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed: 14671022] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Landsberg erecta.
[8]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ131205 mRNA. Translation: CAA10320.1. AC008007 Genomic DNA. Translation: AAF69549.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE32910.1. AF324670 mRNA. Translation: AAG40021.1. AF339684 mRNA. Translation: AAK00366.1. AY062580 mRNA. Translation: AAL32658.1. AY128783 mRNA. Translation: AAM91183.1. AY087304 mRNA. Translation: AAM64855.1.
IPI	IPI00543566.
PIR	T51311.
RefSeq	NP_564625.1. NM_104202.2.
UniGene	At.23771.
3D structure databases
ProteinModelPortal	Q9ZP06.
SMR	Q9ZP06. Positions 31-338.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9ZP06. 1 interaction.
STRING	Q9ZP06.
2D gel databases
SWISS-2DPAGE	Q9ZP06.
Proteomic databases
PRIDE	Q9ZP06.
ProMEX	Q9ZP06.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G53240.1; AT1G53240.1; AT1G53240.
GeneID	841757.
GenomeReviews	Gene locus AT1G53240 in contig CT485782_GR.
KEGG	ath:AT1G53240.
NMPDR	fig|3702.1.peg.4820.
Organism-specific databases
GeneFarm	2023. 159.
TAIR	At1g53240.
Phylogenomic databases
eggNOG	KOG1494.
GeneTree	EPGT00070000029451.
HOGENOM	HBG566126.
InParanoid	Q9ZP06.
OMA	CSYVQST.
PhylomeDB	Q9ZP06.
ProtClustDB	PLN00106.
Gene expression databases
ArrayExpress	Q9ZP06.
Genevestigator	Q9ZP06.
GermOnline	AT1G53240. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR010097. Malate_DH_type1. 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.
KO	K00026.
PANTHER	PTHR11540:SF1. MDH_euk_g_bac. 1 hit.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMs	TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDHM1_ARATH

Accession

Primary (citable) accession number: Q9ZP06
Secondary accession number(s): Q8LBB9, Q9MAH7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 1999
Last modified:	December 14, 2011
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program