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Reviewed, UniProtKB/Swiss-Prot P85310 (AATM_CATRO)

Last modified May 5, 2009. Version 10. 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:
    Aspartate aminotransferase, mitochondrial
    EC=2.6.1.1
Alternative name(s):
    Transaminase A
    Glutamate oxaloacetate transaminase 2
OrganismCatharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Taxonomic identifier4058 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeCatharanthus

Protein attributes

Sequence length28 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. UniProtKB P00508

Cofactor

Pyridoxal phosphate By similarity. UniProtKB P00508

Subunit structure

Homodimer By similarity. UniProtKB P00508

Subcellular location

Mitochondrion matrix By similarity. UniProtKB P00508

Miscellaneous

In eukaryotes there are cytoplasmic, mitochondrial and chloroplastic isozymes.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionL-aspartate:2-oxoglutarate aminotransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›28›28Aspartate aminotransferase, mitochondrial
PRO_0000312771

Experimental info

Non-adjacent residues13 – 142
Non-terminal residue11
Non-terminal residue281

Sequences

Sequence LengthMass (Da)Tools
P85310-1 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 8D8BE476675B227A

FASTA283,031
        10         20 
DDNGKPYVLP SVRTCGFDFT GAVEDISK 

« Hide

References

[1]Varman P.A.M., Ranjitha Kumari B.D.
Submitted (OCT-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA2.6.1.1. 20471.

Family and domain databases

InterProIPR004838. NHTrfase_class1_PyrdxlP-BS.
[Graphical view]
PROSITEPS00105. AA_TRANSFER_CLASS_1. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAATM_CATRO
AccessionPrimary (citable) accession number: P85310
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 4, 2007
Last modified: May 5, 2009
This is version 10 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