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Protein

2-aminoadipate transaminase

Gene

lysN

Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of an amino group between 2-oxoadipate (2-OA) and glutamate (Glu) to yield alpha-aminodipate (AAA). It can also transaminate glutamate, leucine, and aromatic amino acids. It also contributes in the biosynthesis of other amino acids such as leucine.1 Publication

Catalytic activityi

L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate.1 Publication

Cofactori

Kineticsi

  1. KM=13.3 µM for 2-oxoisovalerate (at 45 degrees Celsius and pH 7.5)2 Publications
  2. KM=24.2 µM for 2-oxoadipate (at 45 degrees Celsius and pH 7.5)2 Publications
  3. KM=28.8 µM for 2-oxoisocaproate (at 45 degrees Celsius and pH 7.5)2 Publications
  4. KM=148.3 µM for 2-oxo-3-methylvalerate (at 45 degrees Celsius and pH 7.5)2 Publications
  5. KM=300 µM for 2-oxoglutarate (at 45 degrees Celsius and pH 8.0)2 Publications
  6. KM=460 µM for glutamate (at 45 degrees Celsius and pH 8.0)2 Publications
  7. KM=810 µM for alpha-aminodipate (at 45 degrees Celsius and pH 8.0)2 Publications
  8. KM=950 µM for leucine (at 45 degrees Celsius and pH 8.0)2 Publications
  9. KM=381 mM for asparate (with 1 mM of 2-oxoglutarate at 45 degrees Celsius and pH 8.0)2 Publications

    Pathwayi: L-lysine biosynthesis via AAA pathway

    This protein is involved in step 5 of the subpathway that synthesizes L-alpha-aminoadipate from 2-oxoglutarate.
    Proteins known to be involved in the 5 steps of the subpathway in this organism are:
    1. Homocitrate synthase (lys20)
    2. no protein annotated in this organism
    3. Homoaconitase large subunit (hacA), Homoaconitase small subunit (hacB)
    4. Homoisocitrate dehydrogenase (hicd)
    5. 2-aminoadipate transaminase (lysN)
    This subpathway is part of the pathway L-lysine biosynthesis via AAA pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-alpha-aminoadipate from 2-oxoglutarate, the pathway L-lysine biosynthesis via AAA pathway and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei23 – 231Recognizes the side-chain carboxyl group of acidic compounds
    Binding sitei40 – 401Substrate; via amide nitrogen2 Publications
    Binding sitei70 – 701Pyridoxal phosphate1 Publication
    Binding sitei174 – 1741Pyridoxal phosphate1 Publication
    Binding sitei174 – 1741Substrate2 Publications
    Binding sitei245 – 2451Pyridoxal phosphate1 Publication
    Binding sitei368 – 3681Substrate2 Publications

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciTTHE262724:GCAT-43-MONOMER.
    BRENDAi2.6.1.39. 2305.
    UniPathwayiUPA00033; UER00031.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-aminoadipate transaminase (EC:2.6.1.39)
    Alternative name(s):
    2-aminoadipate aminotransferase
    Alpha-aminoadipate aminotransferase
    Short name:
    AAA-AT
    Short name:
    AadAT
    Gene namesi
    Name:lysN
    Ordered Locus Names:TT_C0043
    OrganismiThermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
    Taxonomic identifieri262724 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    Proteomesi
    • UP000000592 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 201S → E: Strongly decreases the affinity for AAA and Glu. A mild decrease of affinity is observed for 2-oxoglutarate. Increases the affinity for leucine and 2-oxoisocaproate. 1 Publication
    Mutagenesisi23 – 231R → A: Strongly decreases the affinity for AAA and Glu. A mild decrease of affinity is observed for 2-oxoglutarate which has the same chain length as Glu, but differs by the presence of a 2-oxo group which is not recognized by R-23. Increases the affinity for leucine and 2-oxoisocaproate due to the absence of gamma-carboxyl group. 1 Publication
    Mutagenesisi23 – 231R → Q: Strongly decreases the affinity for AAA and Glu. A mild decrease of affinity is observed for 2-oxoglutarate which has the same chain length as Glu, but differs by the presence of a 2-oxo group which is not recognized by R-23. Increases the affinity for leucine and 2-oxoisocaproate due to the absence of gamma-carboxyl group. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3973972-aminoadipate transaminasePRO_0000389636Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei263 – 2631N6-(pyridoxal phosphate)lysineBy similarity

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Protein-protein interaction databases

    STRINGi262724.TTC0043.

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 94Combined sources
    Helixi12 – 165Combined sources
    Helixi21 – 299Combined sources
    Beta strandi35 – 395Combined sources
    Helixi44 – 463Combined sources
    Helixi49 – 6719Combined sources
    Helixi77 – 8711Combined sources
    Helixi91 – 933Combined sources
    Beta strandi94 – 985Combined sources
    Helixi99 – 11113Combined sources
    Beta strandi117 – 1237Combined sources
    Helixi126 – 1338Combined sources
    Beta strandi138 – 1458Combined sources
    Helixi151 – 16010Combined sources
    Beta strandi166 – 1683Combined sources
    Turni174 – 1763Combined sources
    Helixi182 – 19514Combined sources
    Beta strandi199 – 2024Combined sources
    Turni204 – 2074Combined sources
    Beta strandi209 – 2135Combined sources
    Helixi218 – 2258Combined sources
    Beta strandi230 – 2367Combined sources
    Turni237 – 2404Combined sources
    Helixi242 – 2443Combined sources
    Beta strandi247 – 2504Combined sources
    Helixi253 – 26715Combined sources
    Helixi272 – 28211Combined sources
    Turni283 – 2853Combined sources
    Helixi286 – 31126Combined sources
    Beta strandi316 – 3183Combined sources
    Beta strandi322 – 3309Combined sources
    Helixi337 – 34610Combined sources
    Beta strandi349 – 3546Combined sources
    Helixi355 – 3573Combined sources
    Beta strandi366 – 3705Combined sources
    Beta strandi372 – 3743Combined sources
    Helixi376 – 39621Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EGYX-ray2.67A/B/C/D1-397[»]
    2Z1YX-ray1.75A/B1-397[»]
    2ZP7X-ray2.26A/B/C/D/E/F1-397[»]
    2ZYJX-ray1.67A/B1-397[»]
    3CBFX-ray1.67A/B1-397[»]
    ProteinModelPortaliQ72LL6.
    SMRiQ72LL6. Positions 2-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ72LL6.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni100 – 1012Pyridoxal phosphate binding
    Regioni202 – 2054Pyridoxal phosphate binding
    Regioni235 – 2373Pyridoxal phosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105C1I. Bacteria.
    COG1167. LUCA.
    KOiK05825.
    OMAiRLNFTYV.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q72LL6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKPLSWSEAF GKGAGRIQAS TIRELLKLTQ RPGILSFAGG LPAPELFPKE
    60 70 80 90 100
    EAAEAAARIL REKGEVALQY SPTEGYAPLR AFVAEWIGVR PEEVLITTGS
    110 120 130 140 150
    QQALDLVGKV FLDEGSPVLL EAPSYMGAIQ AFRLQGPRFL TVPAGEEGPD
    160 170 180 190 200
    LDALEEVLKR ERPRFLYLIP SFQNPTGGLT PLPARKRLLQ MVMERGLVVV
    210 220 230 240 250
    EDDAYRELYF GEARLPSLFE LAREAGYPGV IYLGSFSKVL SPGLRVAFAV
    260 270 280 290 300
    AHPEALQKLV QAKQGADLHT PMLNQMLVHE LLKEGFSERL ERVRRVYREK
    310 320 330 340 350
    AQAMLHALDR EVPKEVRYTR PKGGMFVWME LPKGLSAEGL FRRALEENVA
    360 370 380 390
    FVPGGPFFAN GGGENTLRLS YATLDREGIA EGVRRLGRAL KGLLALV
    Length:397
    Mass (Da):43,845
    Last modified:July 5, 2004 - v1
    Checksum:iA40FEA8E91D0AFDD
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE017221 Genomic DNA. Translation: AAS80391.1.
    RefSeqiWP_011172501.1. NC_005835.1.

    Genome annotation databases

    EnsemblBacteriaiAAS80391; AAS80391; TT_C0043.
    KEGGitth:TTC0043.
    PATRICi23950469. VBITheThe54392_0043.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE017221 Genomic DNA. Translation: AAS80391.1.
    RefSeqiWP_011172501.1. NC_005835.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EGYX-ray2.67A/B/C/D1-397[»]
    2Z1YX-ray1.75A/B1-397[»]
    2ZP7X-ray2.26A/B/C/D/E/F1-397[»]
    2ZYJX-ray1.67A/B1-397[»]
    3CBFX-ray1.67A/B1-397[»]
    ProteinModelPortaliQ72LL6.
    SMRiQ72LL6. Positions 2-397.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi262724.TTC0043.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAS80391; AAS80391; TT_C0043.
    KEGGitth:TTC0043.
    PATRICi23950469. VBITheThe54392_0043.

    Phylogenomic databases

    eggNOGiENOG4105C1I. Bacteria.
    COG1167. LUCA.
    KOiK05825.
    OMAiRLNFTYV.

    Enzyme and pathway databases

    UniPathwayiUPA00033; UER00031.
    BioCyciTTHE262724:GCAT-43-MONOMER.
    BRENDAi2.6.1.39. 2305.

    Miscellaneous databases

    EvolutionaryTraceiQ72LL6.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiLYSN_THET2
    AccessioniPrimary (citable) accession number: Q72LL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: July 5, 2004
    Last modified: September 7, 2016
    This is version 78 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism.

    Keywords - Technical termi

    3D-structure, Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.