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Protein Overview: AAT_ECOLI

General Information:
Name(s) found: AAT_ECOLI [Swiss-Prot]
Description(s) found:
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  • gi|71041932|pdb|1X2A|B Chain B, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-D-Glutamic Acid [NCBI NR]
  • gi|71041931|pdb|1X2A|A Chain A, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-D-Glutamic Acid [NCBI NR]
  • gi|71041930|pdb|1X29|B Chain B, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-2-Methyl-L-Glutamic Acid [NCBI NR]
  • gi|71041929|pdb|1X29|A Chain A, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-2-Methyl-L-Glutamic Acid [NCBI NR]
  • gi|71041928|pdb|1X28|B Chain B, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-L-Glutamic Acid [NCBI NR]
  • gi|71041927|pdb|1X28|A Chain A, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-L-Glutamic Acid [NCBI NR]
  • pir||XNECD aspartate transaminase (EC 2.6.1.1) aspC [validated] - Escherichia coli (strain K-12) [NCBI NR]
  • gi|640164|pdb|1ARS| Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Complexed With Pyridoxal-5'-Phosphate [NCBI NR]
  • gi|640153|pdb|1AMS| Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Complexed With Pyridoxamine 5'-Phosphate And Glutarate [NCBI NR]
  • gi|640152|pdb|1AMR| Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Complexed With Pyridoxamine 5'-Phosphate And Maleate [NCBI NR]
  • gi|640151|pdb|1AMQ| Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Complexed With Pyridoxamine 5'-Phosphate [NCBI NR]
  • gi|515081|pdb|1ASE| Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Wild Type Complexed With Pyridoxal-5'-Phosphate-N-Oxide And Maleate [NCBI NR]
  • gi|515080|pdb|1ASD| Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Wild Type Complexed With N-Methyl-Pyridoxal-5'-Phosphate And Maleate [NCBI NR]
  • gi|515077|pdb|1ASA| Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Wild Type Complexed With Pyridoxal-5'-Phosphate And Maleate [NCBI NR]
  • gi|493836|pdb|1ASN|B Chain B, Crystal Structures Of Escherichia Coli Aspartate Aminotransferase In Two Conformations: Comparison Of An Unliganded Open And Two Liganded Closed Forms [NCBI NR]
  • gi|493835|pdb|1ASN|A Chain A, Crystal Structures Of Escherichia Coli Aspartate Aminotransferase In Two Conformations: Comparison Of An Unliganded Open And Two Liganded Closed Forms [NCBI NR]
  • gi|493834|pdb|1ASM|B Chain B, Crystal Structures Of Escherichia Coli Aspartate Aminotransferase In Two Conformations: Comparison Of An Unliganded Open And Two Liganded Closed Forms [NCBI NR]
  • gi|493833|pdb|1ASM|A Chain A, Crystal Structures Of Escherichia Coli Aspartate Aminotransferase In Two Conformations: Comparison Of An Unliganded Open And Two Liganded Closed Forms [NCBI NR]
  • gi|493832|pdb|1ASL|B Chain B, Crystal Structures Of Escherichia Coli Aspartate Aminotransferase In Two Conformations: Comparison Of An Unliganded Open And Two Liganded Closed Forms [NCBI NR]
  • gi|493831|pdb|1ASL|A Chain A, Crystal Structures Of Escherichia Coli Aspartate Aminotransferase In Two Conformations: Comparison Of An Unliganded Open And Two Liganded Closed Forms [NCBI NR]
  • gi|442601|pdb|1AAW| Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Wild Type Complex With Pyridoxal-5'-Phosphate [NCBI NR]
  • gi|41013|emb|CAA29333.1| unnamed protein product [Escherichia coli] [NCBI NR]
  • gi|41011|emb|CAA27279.1| unnamed protein product [Escherichia coli] [NCBI NR]
  • gi|157830056|pdb|1ASE|A Chain A, The Structure Of Wild Type E. Coli Aspartate Aminotransferase Reconstituted With Plp-N-Oxide [NCBI NR]
  • gi|157830055|pdb|1ASD|A Chain A, The Structure Of Wild Type E. Coli Aspartate Aminotransferase Reconstituted With N-Meplp [NCBI NR]
  • gi|157830052|pdb|1ASA|A Chain A, The Structural Basis For The Reduced Activity Of The Y226f(Y225f) Active Site Mutant Of E. Coli Aspartate Aminotransferase [NCBI NR]
  • gi|157830042|pdb|1ART|A Chain A, X-Ray Crystallographic Study Of Pyridoxal 5'-Phosphate-Type Aspartate Aminotransferases From Escherichia Coli In Open And Closed Form [NCBI NR]
  • gi|157830041|pdb|1ARS|A Chain A, X-Ray Crystallographic Study Of Pyridoxal 5'-Phosphate-Type Aspartate Aminotransferases From Escherichia Coli In Open And Closed Form [NCBI NR]
  • gi|157829973|pdb|1AMS|A Chain A, X-Ray Crystallographic Study Of Pyridoxamine 5'-Phosphate- Type Aspartate Aminotransferases From Escherichia Coli In Three Forms [NCBI NR]
  • gi|157829972|pdb|1AMR|A Chain A, X-Ray Crystallographic Study Of Pyridoxamine 5'-Phosphate- Type Aspartate Aminotransferases From Escherichia Coli In Three Forms [NCBI NR]
  • gi|157829971|pdb|1AMQ|A Chain A, X-Ray Crystallographic Study Of Pyridoxamine 5'-Phosphate- Type Aspartate Aminotransferases From Escherichia Coli In Three Forms [NCBI NR]
  • gi|157829774|pdb|1AAW|A Chain A, The Structural Basis For The Altered Substrate Specificity Of The R292d Active Site Mutant Of Aspartate Aminotransferase From E. Coli [NCBI NR]
  • gi|1311174|pdb|1ARG|B Chain B, Aspartate Aminotransferase, Phospho-5'-Pyridoxyl Aspartate Complex [NCBI NR]
  • gi|1311173|pdb|1ARG|A Chain A, Aspartate Aminotransferase, Phospho-5'-Pyridoxyl Aspartate Complex [NCBI NR]
  • gi|12084333|pdb|1CQ8|A Chain A, Aspartate Aminotransferase (E.C. 2.6.1.1) Complexed With C6- Pyridoxal-5p-Phosphate [NCBI NR]
  • gi|12084332|pdb|1CQ7|A Chain A, Aspartate Aminotransferase (E.C. 2.6.1.1) Complexed With C5- Pyridoxal-5p-Phosphate [NCBI NR]
  • gi|12084331|pdb|1CQ6|A Chain A, Aspartate Aminotransferase Complex With C4-Pyridoxal-5p- Phosphate [NCBI NR]
  • gi|12084330|pdb|1C9C|A Chain A, Aspartate Aminotransferase Complexed With C3-Pyridoxal-5'- Phosphate [NCBI NR]
  • gi|112989|sp|P00509.1|AAT_ECOLI RecName: Full=Aspartate aminotransferase; Short=AspAT; AltName: Full=Transaminase A [NCBI NR]
  • Aspartate aminotransferase (EC 2.6.1.1) (Transaminase A) (ASPAT) - Escherichia coli [Swiss-Prot]
  • aspartate aminotransferase; aspartate aminotransferase, PLP-dependent [Escherichia coli K12]gi|1787159|gb|AAC74014.1| aspartate aminotransferase; aspartate aminotransferase, PLP-dependent [Escherichia coli K12]gi|41011|emb|CAA27279.1| unnamed protein pr [nrdb_11152004_Chlamydomonas]
  • Aspartate aminotransferase (ASPAT) (Transaminase A) [NCBI-RefSeq_human_na_08-09-2006_reversed.fasta]
  • Chain A, Aspartate Aminotransferase (E.C.2.6.1.1) (Wild Type, Pyridoxal-5'-Phosphate Form) Complex With Sulfate [nr-271106-contam.fasta]
  • Chain B, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-D-Glutamic Acid [nr-271106-contam.fasta]
  • Chain B, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-2-Methyl-L-Glutamic Acid [nr-271106-contam.fasta]
  • unnamed protein product [Escherichia coli] [nr-271106-contam.fasta]
  • Chain B, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-L-Glutamic Acid [nr-271106-contam.fasta]
  • Chain B, Aspartate Aminotransferase (E.C.2.6.1.1) (Wild Type) Complex With 2-Methylaspartyl-Pyridoxal-5'-Phosphate [nr-271106-contam.fasta]
  • Chain B, Aspartate Aminotransferase (E.C.2.6.1.1) (Wild Type, Pyridoxal-5'-Phosphate Form) Complex With Sulfate [nr-271106-contam.fasta]
  • Chain A, Aspartate Aminotransferase Complexed With C3-Pyridoxal-5'- Phosphate [nr-271106-contam.fasta]
  • Chain A, Aspartate Aminotransferase (E.C.2.6.1.1) (Wild Type) Complex With 2-Methylaspartyl-Pyridoxal-5'-Phosphate [nr-271106-contam.fasta]
  • Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Complexed With Pyridoxal-5'-Phosphate [nr-271106-contam.fasta]
  • Chain A, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-2-Methyl-L-Glutamic Acid [nr-271106-contam.fasta]
  • Chain A, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-L-Glutamic Acid [nr-271106-contam.fasta]
  • Chain B, Aspartate Aminotransferase, Phospho-5'-Pyridoxyl Aspartate Complex [nr-271106-contam.fasta]
  • Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Wild Type Complexed With Pyridoxal-5'-Phosphate And Maleate [nr-271106-contam.fasta]
  • Chain A, Aspartate Aminotransferase (E.C.2.6.1.1) (Wild Type, Pyridoxal-5'-Phosphate Form) Complex With Maleate [nr-271106-contam.fasta]
  • Chain A, Aspartate Aminotransferase (E.C. 2.6.1.1) Complexed With C5- Pyridoxal-5p-Phosphate [nr-271106-contam.fasta]
  • Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Wild Type Complex With Pyridoxal-5'-Phosphate [nr-271106-contam.fasta]
  • Chain A, Crystal Structure Of E.Coli Aspat Complexed With N- Phosphopyridoxyl-D-Glutamic Acid [nr-271106-contam.fasta]
  • Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Wild Type Complexed With N-Methyl-Pyridoxal-5'-Phosphate And Maleate [nr-271106-contam.fasta]
  • Chain B, Aspartate Aminotransferase (E.C.2.6.1.1) (Wild Type, Pyridoxal-5'-Phosphate Form) Complex With Maleate [nr-271106-contam.fasta]
  • Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Complexed With Pyridoxamine 5'-Phosphate [nr-271106-contam.fasta]
  • Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Complexed With Pyridoxamine 5'-Phosphate And Maleate [nr-271106-contam.fasta]
  • Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Complexed With Pyridoxamine 5'-Phosphate And Glutarate [nr-271106-contam.fasta]
  • Chain A, Aspartate Aminotransferase Complex With C4-Pyridoxal-5p- Phosphate [nr-271106-contam.fasta]
  • Chain A, Aspartate Aminotransferase, Phospho-5'-Pyridoxyl Aspartate Complex [nr-271106-contam.fasta]
  • Chain A, Aspartate Aminotransferase (E.C. 2.6.1.1) Complexed With C6- Pyridoxal-5p-Phosphate [nr-271106-contam.fasta]
  • Chain , Aspartate Aminotransferase (E.C.2.6.1.1) Wild Type Complexed With Pyridoxal-5'-Phosphate-N-Oxide And Maleate [nr-271106-contam.fasta]
  • Aspartate aminotransferase OS=Escherichia coli (strain K12) GN=aspC PE=1 SV=1 [uniprot-Ecoli-reviewed-110511.fasta]
    • Organism: Escherichia coli
    Length: 396 amino acids

    Gene Ontology:
    Cellular Component: NONE FOUND
    Biological Process: NONE FOUND
    Molecular Function: NONE FOUND


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MFENITAAPA DPILGLADLF RADERPGKIN LGIGVYKDET GKTPVLTSVK KAEQYLLENE  60
   61 TTKNYLGIDG IPEFGRCTQE LLFGKGSALI NDKRARTAQT PGGTGALRVA ADFLAKNTSV 120
  121 KRVWVSNPSW PNHKSVFNSA GLEVREYAYY DAENHTLDFD ALINSLNEAQ AGDVVLFHGC 180
  181 CHNPTGIDPT LEQWQTLAQL SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAAMHKELIV 240
  241 ASSYSKNFGL YNERVGACTL VAADSETVDR AFSQMKAAIR ANYSNPPAHG ASVVATILSN 300
  301 DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF SGLTKEQVLR 360
  361 LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL

    Protein Complex Data

    No complex found for this protein.

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    SHOWING SINGLE HITS. [ Hide Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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    No microscopy data found in the PDR for this protein.

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..396] PSI-BLAST 90.30103 THE STRUCTURAL BASIS FOR THE ALTERED SUBSTRATE SPECIFICITY OF THE R292D ACTIVE SITE MUTANT OF ASPARTATE AMINOTRANSFERASE FROM E. COLI

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • L-aspartate:2-oxoglutarate aminotransferase activity
    		•  5.03677961292867 bayes_pls_golite062009
  • catalytic activity
    		•  2.29878871754893 bayes_pls_golite062009
  • transferase activity
    		•  1.44093490824786 bayes_pls_golite062009
  • transferase activity, transferring nitrogenous groups
    		•  1.28316822767388 bayes_pls_golite062009
  • transaminase activity
    		•  1.24990480711889 bayes_pls_golite062009
  • pyridoxal phosphate binding
    		•  0.16957228630576 bayes_pls_golite062009
  • vitamin B6 binding
    		•  0.16957228630576 bayes_pls_golite062009
  • aromatic-amino-acid:2-oxoglutarate aminotransferase activity
    		•  0.0916183433120769 bayes_pls_golite062009
  • cystathionine beta-lyase activity
    		•  0.0833010353195099 bayes_pls_golite062009


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.99

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle