Aspartate aminotransferase, mitochondrial

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

Miscellaneous

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• 2-oxoglutarate

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  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + L-aspartate

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  = L-glutamate

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  + oxaloacetate

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  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.7

    "Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain."
    Guidetti P., Amori L., Sapko M.T., Okuno E., Schwarcz R.
    J. Neurochem. 102:103-111(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: PROTEIN SEQUENCE OF 30-42, CATALYTIC ACTIVITY, FUNCTION.
  EC:2.6.1.1
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.7

    "Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain."
    Guidetti P., Amori L., Sapko M.T., Okuno E., Schwarcz R.
    J. Neurochem. 102:103-111(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: PROTEIN SEQUENCE OF 30-42, CATALYTIC ACTIVITY, FUNCTION.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

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  2-oxoglutarate

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  • See the description of this molecule in ChEBI.

  zoom

  +

  L-aspartate

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  • See the description of this molecule in ChEBI.

  zoom

  =

  L-glutamate

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  +

  oxaloacetate

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  zoom
• 2-oxoglutarate

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  + L-kynurenine

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  = 4-(2-aminophenyl)-2,4-dioxobutanoate

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  + L-glutamate

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  • See the description of this molecule in ChEBI.

  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.7

    "Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain."
    Guidetti P., Amori L., Sapko M.T., Okuno E., Schwarcz R.
    J. Neurochem. 102:103-111(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: PROTEIN SEQUENCE OF 30-42, CATALYTIC ACTIVITY, FUNCTION.
  EC:2.6.1.7
  • Search proteins in UniProtKB for this EC number.
  • See the description of this EC number in ENZYME.
  1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.7

    "Mitochondrial aspartate aminotransferase: a third kynurenate-producing enzyme in the mammalian brain."
    Guidetti P., Amori L., Sapko M.T., Okuno E., Schwarcz R.
    J. Neurochem. 102:103-111(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: PROTEIN SEQUENCE OF 30-42, CATALYTIC ACTIVITY, FUNCTION.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

  . Show »« Hide
  2-oxoglutarate

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  • See the description of this molecule in ChEBI.

  zoom

  +

  L-kynurenine

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  zoom

  =

  4-(2-aminophenyl)-2,4-dioxobutanoate

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  zoom

  +

  L-glutamate

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  • See the description of this molecule in ChEBI.

  zoom

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• amino acid binding Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase."
    Oses-Prieto J.A., Bengoechea-Alonso M.T., Artigues A., Iriarte A., Martinez-Carrion M.
    J Biol Chem 278:49988-49999(2003) [PubMed] [Europe PMC] [Abstract]
• carboxylic acid binding Source: RGDInferred from direct assayⁱ
  • "The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase."
    Oses-Prieto J.A., Bengoechea-Alonso M.T., Artigues A., Iriarte A., Martinez-Carrion M.
    J Biol Chem 278:49988-49999(2003) [PubMed] [Europe PMC] [Abstract]
• enzyme binding Source: RGDInferred from direct assayⁱ
  • "Regulation of aminotransferase-glutamate dehydrogenase interactions by carbamyl phosphate synthase-I, Mg2+ plus leucine versus citrate and malate."
    Fahien L.A., Kmiotek E.H., Woldegiorgis G., Evenson M., Shrago E., Marshall M.
    J Biol Chem 260:6069-6079(1985) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Release of pyridoxal 5'-phosphate upon unfolding of mitochondrial aspartate aminotransferase."
    Wu T.H., Oses-Prieto J.A., Iriarte A., Martinez-Carrion M.
    Biochim Biophys Acta 1647:315-320(2003) [PubMed] [Europe PMC] [Abstract]
• kynurenine-oxoglutarate transaminase activity Source: UniProtKB-EC
• L-aspartate:2-oxoglutarate aminotransferase activity Source: RGDInferred from direct assayⁱ
  • "Possible mechanism for the decrease of mitochondrial aspartate aminotransferase activity in ischemic and hypoxic rat retinas."
    Endo S., Ishiguro S., Tamai M.
    Biochim Biophys Acta 1450:385-396(1999) [PubMed] [Europe PMC] [Abstract]
  • "The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase."
    Oses-Prieto J.A., Bengoechea-Alonso M.T., Artigues A., Iriarte A., Martinez-Carrion M.
    J Biol Chem 278:49988-49999(2003) [PubMed] [Europe PMC] [Abstract]
• phospholipid binding Source: RGDInferred from direct assayⁱ
  • "Regulation of aminotransferase-glutamate dehydrogenase interactions by carbamyl phosphate synthase-I, Mg2+ plus leucine versus citrate and malate."
    Fahien L.A., Kmiotek E.H., Woldegiorgis G., Evenson M., Shrago E., Marshall M.
    J Biol Chem 260:6069-6079(1985) [PubMed] [Europe PMC] [Abstract]
• pyridoxal phosphate binding Source: RGDInferred from direct assayⁱ
  • "The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase."
    Oses-Prieto J.A., Bengoechea-Alonso M.T., Artigues A., Iriarte A., Martinez-Carrion M.
    J Biol Chem 278:49988-49999(2003) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• 2-oxoglutarate metabolic process Source: UniProtKB
• aspartate biosynthetic process Source: RGD
• aspartate catabolic process Source: RGD
• aspartate metabolic process Source: RGDInferred from mutant phenotypeⁱ
  • "Release of pyridoxal 5'-phosphate upon unfolding of mitochondrial aspartate aminotransferase."
    Wu T.H., Oses-Prieto J.A., Iriarte A., Martinez-Carrion M.
    Biochim Biophys Acta 1647:315-320(2003) [PubMed] [Europe PMC] [Abstract]
• cellular amino acid metabolic process Source: RGDInferred from direct assayⁱ
  • "The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase."
    Oses-Prieto J.A., Bengoechea-Alonso M.T., Artigues A., Iriarte A., Martinez-Carrion M.
    J Biol Chem 278:49988-49999(2003) [PubMed] [Europe PMC] [Abstract]
• dicarboxylic acid metabolic process Source: RGDInferred from direct assayⁱ
  • "The nature of the rate-limiting steps in the refolding of the cofactor-dependent protein aspartate aminotransferase."
    Oses-Prieto J.A., Bengoechea-Alonso M.T., Artigues A., Iriarte A., Martinez-Carrion M.
    J Biol Chem 278:49988-49999(2003) [PubMed] [Europe PMC] [Abstract]
• fatty acid transport Source: RGD
• female pregnancy Source: RGD <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • "The effect of gestational age on expression of genes involved in uptake, trafficking and synthesis of fatty acids in the rat placenta."
    Rodriguez-Cruz M., Gonzalez R.S., Maldonado J., Lopez-Alarcon M., Bernabe-Garcia M.
    Gene 591:403-410(2016) [PubMed] [Europe PMC] [Abstract]
• glutamate catabolic process to 2-oxoglutarate Source: RGDInferred from direct assayⁱ
  • "Regulation of 2-oxoglutarate metabolism in rat liver by NADP-isocitrate dehydrogenase and aspartate aminotransferase."
    Rakhmanova T.I., Popova T.N.
    Biochemistry (Mosc) 71:211-217(2006) [PubMed] [Europe PMC] [Abstract]
• glutamate catabolic process to aspartate Source: RGD
• glutamate metabolic process Source: UniProtKB
• lactation Source: RGDInferred from expression patternⁱ
  • "Change in the Lipid Transport Capacity of the Liver and Blood during Reproduction in Rats."
    Zhang Y., Kallenberg C., Hyatt H.W., Kavazis A.N., Hood W.R.
    Front Physiol 8:517-517(2017) [PubMed] [Europe PMC] [Abstract]
• oxaloacetate metabolic process Source: RGDInferred from direct assayⁱ
  • "Regulation of 2-oxoglutarate metabolism in rat liver by NADP-isocitrate dehydrogenase and aspartate aminotransferase."
    Rakhmanova T.I., Popova T.N.
    Biochemistry (Mosc) 71:211-217(2006) [PubMed] [Europe PMC] [Abstract]
• response to ethanol Source: RGD
• response to insulin Source: RGDInferred from expression patternⁱ
  • "Fatty acid transport proteins chronically relocate to the transverse-tubules in muscle from obese Zucker rats but are resistant to further insulin-induced translocation."
    Stefanyk L.E., Bonen A., Dyck D.J.
    Metabolism 62:1296-1304(2013) [PubMed] [Europe PMC] [Abstract]
• response to morphine Source: RGDInferred from expression patternⁱ
  • "Proteomic analysis of post-nuclear supernatant fraction and percoll-purified membranes prepared from brain cortex of rats exposed to increasing doses of morphine."
    Ujcikova H., Eckhardt A., Kagan D., Roubalova L., Svoboda P.
    Proteome Sci 12:11-11(2014) [PubMed] [Europe PMC] [Abstract]
• response to muscle activity Source: RGDInferred from expression patternⁱ
  • "Acute endurance exercise increases plasma membrane fatty acid transport proteins in rat and human skeletal muscle."
    Bradley N.S., Snook L.A., Jain S.S., Heigenhauser G.J., Bonen A., Spriet L.L.
    Am J Physiol Endocrinol Metab 302:E183-9(2012) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• enzyme binding Source: RGDInferred from direct assayⁱ
  • "Regulation of aminotransferase-glutamate dehydrogenase interactions by carbamyl phosphate synthase-I, Mg2+ plus leucine versus citrate and malate."
    Fahien L.A., Kmiotek E.H., Woldegiorgis G., Evenson M., Shrago E., Marshall M.
    J Biol Chem 260:6069-6079(1985) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: RGDInferred from mutant phenotypeⁱ
  • "Release of pyridoxal 5'-phosphate upon unfolding of mitochondrial aspartate aminotransferase."
    Wu T.H., Oses-Prieto J.A., Iriarte A., Martinez-Carrion M.
    Biochim Biophys Acta 1647:315-320(2003) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MALLHSGRVL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA 
        60         70         80         90        100
FKRDTNSKKM NLGVGAYRDD NGKPYVLPSV RKAEAQIAGK NLDKEYLPIG 
       110        120        130        140        150
GLADFCKASA ELALGENSEV LKSGRFVTVQ TISGTGALRV GASFLQRFFK 
       160        170        180        190        200
FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR YYDPKTCGFD FSGALEDISK 
       210        220        230        240        250
IPEQSVLLLH ACAHNPTGVD PRPEQWKEMA AVVKKKNLFA FFDMAYQGFA 
       260        270        280        290        300
SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE 
       310        320        330        340        350
AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR 
       360        370        380        390        400
IISMRTQLVS NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV 
       410        420        430
YMTKDGRISV AGVTSGNVGY LAHAIHQVTK                       

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. SIMILARITY comments
   Index of protein domains and families