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Q9ZP06 (MDHM1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length341 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processTricarboxylic acid cycle
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular carbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

defense response to bacterium

Inferred from expression pattern PubMed 17028151. Source: TAIR

malate metabolic process

Inferred from electronic annotation. Source: InterPro

response to cadmium ion

Inferred from expression pattern PubMed 16502469. Source: TAIR

response to cold

Inferred from expression pattern PubMed 14535880. Source: TAIR

response to salt stress

Inferred from expression pattern PubMed 17916636. Source: TAIR

tricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapoplast

Inferred from direct assay PubMed 21798377. Source: TAIR

cell wall

Inferred from direct assay PubMed 16287169. Source: TAIR

chloroplast

Inferred from direct assay PubMed 18431481. Source: TAIR

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay Ref.6PubMed 11743115PubMed 12492832Ref.7PubMed 15276431PubMed 18385124PubMed 22923678. Source: TAIR

   Molecular_functionL-malate dehydrogenase activity

Inferred from mutant phenotype PubMed 20876337. Source: TAIR

copper ion binding

Inferred from direct assay PubMed 20018591. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2222Mitochondrion Ref.6
Chain23 – 341319Malate dehydrogenase 1, mitochondrial
PRO_0000018622

Regions

Nucleotide binding36 – 427NAD By similarity
Nucleotide binding145 – 1473NAD By similarity

Sites

Active site2051Proton acceptor By similarity
Binding site621NAD By similarity
Binding site1091Substrate By similarity
Binding site1151Substrate By similarity
Binding site1221NAD By similarity
Binding site1471Substrate By similarity
Binding site1811Substrate By similarity
Binding site2561NAD By similarity

Experimental info

Sequence conflict171V → A in AAM64855. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9ZP06 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: D035C4C38785BE57

FASTA34135,804
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: 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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRT51311.
RefSeqNP_564625.1. NM_104202.2.
UniGeneAt.23771.

3D structure databases

ProteinModelPortalQ9ZP06.
SMRQ9ZP06. Positions 31-338.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid26982. 1 interaction.
IntActQ9ZP06. 1 interaction.

2D gel databases

SWISS-2DPAGEQ9ZP06.

Proteomic databases

PaxDbQ9ZP06.
PRIDEQ9ZP06.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G53240.1; AT1G53240.1; AT1G53240.
GeneID841757.
KEGGath:AT1G53240.

Organism-specific databases

GeneFarm2023. 159.
TAIRAT1G53240.

Phylogenomic databases

eggNOGCOG0039.
HOGENOMHOG000213792.
InParanoidQ9ZP06.
KOK00026.
OMAYVQSTIT.
PhylomeDBQ9ZP06.

Enzyme and pathway databases

BioCycARA:AT1G53240-MONOMER.
MetaCyc:AT1G53240-MONOMER.

Gene expression databases

GenevestigatorQ9ZP06.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.110.10. 1 hit.
InterProIPR001557. 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]
PANTHERPTHR11540. PTHR11540. 1 hit.
PfamPF02866. Ldh_1_C. 1 hit.
PF00056. Ldh_1_N. 1 hit.
[Graphical view]
PIRSFPIRSF000102. Lac_mal_DH. 1 hit.
SUPFAMSSF56327. SSF56327. 1 hit.
TIGRFAMsTIGR01772. MDH_euk_gproteo. 1 hit.
PROSITEPS00068. MDH. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMDHM1_ARATH
AccessionPrimary (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: June 11, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names