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Reviewed, UniProtKB/Swiss-Prot P37225 (MAON_SOLTU)

Last modified November 25, 2008. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NAD-dependent malic enzyme 59 kDa isoform, mitochondrial
      Short name=NAD-ME
    EC=1.1.1.39
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length601 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(+) = pyruvate + CO(2) + NADH.

Cofactor

Divalent metal cations. Prefers magnesium or manganese By similarity.

Subunit structure

Heterodimer of two related subunits.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the malic enzymes family.

Ontologies

Keywords

   Cellular componentMitochondrion
   DomainTransit peptide
   LigandMetal-binding
NAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processmalate metabolic process

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionNAD binding

Inferred from electronic annotation. Source: InterPro

malate dehydrogenase (decarboxylating) activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1818Mitochondrion
Chain19 – 601583NAD-dependent malic enzyme 59 kDa isoform, mitochondrial
PRO_0000018544

Sites

Active site1291Proton donor By similarity
Active site2001Proton acceptor By similarity
Metal binding2711Divalent metal cation By similarity
Metal binding2721Divalent metal cation By similarity
Metal binding2951Divalent metal cation By similarity
Binding site1821NAD By similarity
Binding site2951NAD By similarity
Binding site4441NAD By similarity
Site2951Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P37225-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: D6C2A128CC9E971C

FASTA60166,272
        10         20         30         40         50         60 
MWRVARSAAS TFRRTRRLST AISAPCIVHK RGADILHDPW FNKDTGFPMT ERDRLGLRGL 

        70         80         90        100        110        120 
LPPRVISFEQ QYDRFMESFR SLEKNTEGQP DSVVSLAKWR ILNRLHDRNE TLYYRVLIDN 

       130        140        150        160        170        180 
IKDFAPIIYT PTVGLVCQNY SGLFRRPRGM YFSAKDKGEM MSMIFNWPST QVDMIVLTDG 

       190        200        210        220        230        240 
SRILGLGDLG VQGIGIPIGK LDMYVAAAGI NPQRVLPVML DVGTNNQKLL EDPLYLGLRQ 

       250        260        270        280        290        300 
PRLEGEEYLS IVDEFVEAVH ARWPKAVVQF EDFQAKWAFE TLDRYRKKFC MFNDDIQGTA 

       310        320        330        340        350        360 
GVALAGLLGT VRAQGRPLTD FANQKIVVVG AGSAGLGVLK MALQAVSRMT GPSADPHFFL 

       370        380        390        400        410        420 
LDKNGLITKD RKDIDPAALP FAKAHHEIEG LGLQEGAGLA EVVKKVKPHV LLGLSGVGGI 

       430        440        450        460        470        480 
FHEEVLRAMK ESDSVRPAIF AMSNPTNNAE CCPVDAFKLA GEDIVFASGS PFANVDLGNG 

       490        500        510        520        530        540 
KIGHVNQANN MYLFPGIGLG ALLSGARNIS DTMLEAAAEC LASYMSDDEI NRGILYPSID 

       550        560        570        580        590        600 
DIRDITAEVG AAVLRAAVAE DLAEGHGDVG VKELQHMSKE ETIEHVRQNM WYPVYGPLVH 


E 

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References

[1]"Plant mitochondrial NAD+-dependent malic enzyme. cDNA cloning, deduced primary structure of the 59- and 62-kDa subunits, import, gene complexity and expression analysis."
Winning B.M., Bourguignon J., Leaver C.J.
J. Biol. Chem. 269:4780-4786(1994) [PubMed: 8106447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Desiree.
Tissue: Leaf.

Cross-references

Sequence databases

Z23002 mRNA. Translation: CAA80547.1.
PIRA53318.

3D structure databases

HSSPHSSP built from PDB template 1LLQ based on UniProtKB P27443.
ModBaseSearch...

Protein-protein interaction databases

IntActP37225.

Family and domain databases

InterProIPR015884. Malic_enzyme_CS.
IPR012301. Malic_N.
IPR012302. Malic_NAD_bd.
IPR001891. Malic_OxRdtase.
IPR016040. NAD(P)-bd.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00390. malic. 1 hit.
PF03949. Malic_M. 1 hit.
[Graphical view]
PRINTSPR00072. MALOXRDTASE.
PROSITEPS00331. MALIC_ENZYMES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMAON_SOLTU
AccessionPrimary (citable) accession number: P37225
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 25, 2008
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents