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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)DescriptionActionsGraphical viewLength
    Sitei23Recognizes the side-chain carboxyl group of acidic compounds1
    Binding sitei40Substrate; via amide nitrogen2 Publications1
    Binding sitei70Pyridoxal phosphate1 Publication1
    Binding sitei174Pyridoxal phosphate1 Publication1
    Binding sitei174Substrate2 Publications1
    Binding sitei245Pyridoxal phosphate1 Publication1
    Binding sitei368Substrate2 Publications1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi20S → 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 Publication1
    Mutagenesisi23R → 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 Publication1
    Mutagenesisi23R → 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 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00003896361 – 3972-aminoadipate transaminaseAdd BLAST397

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei263N6-(pyridoxal phosphate)lysineBy similarity1

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Protein-protein interaction databases

    STRINGi262724.TTC0043.

    Structurei

    Secondary structure

    1397
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi6 – 9Combined sources4
    Helixi12 – 16Combined sources5
    Helixi21 – 29Combined sources9
    Beta strandi35 – 39Combined sources5
    Helixi44 – 46Combined sources3
    Helixi49 – 67Combined sources19
    Helixi77 – 87Combined sources11
    Helixi91 – 93Combined sources3
    Beta strandi94 – 98Combined sources5
    Helixi99 – 111Combined sources13
    Beta strandi117 – 123Combined sources7
    Helixi126 – 133Combined sources8
    Beta strandi138 – 145Combined sources8
    Helixi151 – 160Combined sources10
    Beta strandi166 – 168Combined sources3
    Turni174 – 176Combined sources3
    Helixi182 – 195Combined sources14
    Beta strandi199 – 202Combined sources4
    Turni204 – 207Combined sources4
    Beta strandi209 – 213Combined sources5
    Helixi218 – 225Combined sources8
    Beta strandi230 – 236Combined sources7
    Turni237 – 240Combined sources4
    Helixi242 – 244Combined sources3
    Beta strandi247 – 250Combined sources4
    Helixi253 – 267Combined sources15
    Helixi272 – 282Combined sources11
    Turni283 – 285Combined sources3
    Helixi286 – 311Combined sources26
    Beta strandi316 – 318Combined sources3
    Beta strandi322 – 330Combined sources9
    Helixi337 – 346Combined sources10
    Beta strandi349 – 354Combined sources6
    Helixi355 – 357Combined sources3
    Beta strandi366 – 370Combined sources5
    Beta strandi372 – 374Combined sources3
    Helixi376 – 396Combined sources21

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ72LL6.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni100 – 101Pyridoxal phosphate binding2
    Regioni202 – 205Pyridoxal phosphate binding4
    Regioni235 – 237Pyridoxal phosphate binding3

    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:TT_C0043.
    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi262724.TTC0043.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayiUPA00033; UER00031.
    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: November 2, 2016
    This is version 80 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.