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Protein

D-alanine aminotransferase

Gene

dat

Organism
Bacillus sp. (strain YM-1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts on the D-isomers of alanine, leucine, aspartate, glutamate, aminobutyrate, norvaline and asparagine. The enzyme transfers an amino group from a substrate D-amino acid to the pyridoxal phosphate cofactor to form pyridoxamine and an alpha-keto acid in the first half-reaction. The second-half reaction is the reverse of the first, transferring the amino group from the pyridoxamine to a second alpha-keto acid to form the product D-amino acid via a ping-pong mechanism. This is an important process in the formation of D-alanine and D-glutamate, which are essential bacterial cell wall components.2 Publications

Catalytic activityi

D-alanine + 2-oxoglutarate = pyruvate + D-glutamate.2 Publications

Cofactori

pyridoxal 5'-phosphate1 Publication

Absorptioni

Abs(max)=279 nm1 Publication

Holoenzyme exhibits additional strong peaks at 333 nm and 415 nm. Addition of D-alanine causes a decrease in absorbance at 419 nm and an increase at 335 nm.

Kineticsi

  1. KM=2.2 mM for D-alanine1 Publication
  2. KM=5.9 mM for alpha-ketoglutarate1 Publication
  3. KM=2.2 mM for alpha-ketobutyrate1 Publication
  4. KM=2.2 mM for alpha-ketovalerate1 Publication

    pH dependencei

    Optimum pH is 8.3.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei32Substrate1 Publication1
    Binding sitei51Pyridoxal phosphate1 Publication1
    Binding sitei99Substrate1 Publication1
    Binding sitei101Substrate1 Publication1
    Active sitei146Proton acceptor1 Publication1
    Binding sitei178Pyridoxal phosphate1 Publication1

    GO - Molecular functioni

    • D-alanine:2-oxoglutarate aminotransferase activity Source: UniProtKB
    • pyridoxal phosphate binding Source: UniProtKB

    GO - Biological processi

    • D-amino acid biosynthetic process Source: UniProtKB
    • D-amino acid catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BRENDAi2.6.1.21. 691.
    SABIO-RKP19938.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    D-alanine aminotransferase (EC:2.6.1.21)
    Alternative name(s):
    D-amino acid aminotransferase
    D-amino acid transaminase
    Short name:
    DAAT
    D-aspartate aminotransferase
    Gene namesi
    Name:dat
    OrganismiBacillus sp. (strain YM-1)
    Taxonomic identifieri72579 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi178E → K: Loss of transaminase activity and small gain in racemase activity. 1 Publication1
    Mutagenesisi202L → A: Inactivates enzyme. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00001032482 – 283D-alanine aminotransferaseAdd BLAST282

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei146N6-(pyridoxal phosphate)lysine1 Publication1

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1283
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 6Combined sources4
    Beta strandi9 – 12Combined sources4
    Helixi13 – 15Combined sources3
    Helixi23 – 26Combined sources4
    Beta strandi30 – 38Combined sources9
    Beta strandi41 – 44Combined sources4
    Helixi45 – 58Combined sources14
    Helixi67 – 81Combined sources15
    Beta strandi85 – 94Combined sources10
    Beta strandi111 – 118Combined sources8
    Helixi123 – 128Combined sources6
    Beta strandi130 – 136Combined sources7
    Helixi151 – 162Combined sources12
    Beta strandi166 – 172Combined sources7
    Beta strandi175 – 179Combined sources5
    Beta strandi182 – 188Combined sources7
    Beta strandi191 – 194Combined sources4
    Helixi205 – 216Combined sources12
    Helixi228 – 232Combined sources5
    Beta strandi235 – 241Combined sources7
    Turni242 – 244Combined sources3
    Beta strandi245 – 252Combined sources8
    Beta strandi255 – 257Combined sources3
    Turni258 – 260Combined sources3
    Helixi264 – 274Combined sources11

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1A0GX-ray2.00A/B2-283[»]
    1DAAX-ray1.94A/B2-283[»]
    1G2WX-ray2.00A/B2-283[»]
    2DAAX-ray2.10A/B2-283[»]
    2DABX-ray2.00A/B2-283[»]
    3DAAX-ray1.90A/B2-278[»]
    3LQSX-ray1.90A/B2-281[»]
    4DAAX-ray2.40A/B2-278[»]
    5DAAX-ray2.90A/B2-278[»]
    ProteinModelPortaliP19938.
    SMRiP19938.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19938.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    KOiK00824.

    Family and domain databases

    InterProiIPR001544. Aminotrans_IV.
    IPR018300. Aminotrans_IV_CS.
    IPR005784. D_amino_transT.
    [Graphical view]
    PANTHERiPTHR11825. PTHR11825. 1 hit.
    PfamiPF01063. Aminotran_4. 1 hit.
    [Graphical view]
    SUPFAMiSSF56752. SSF56752. 1 hit.
    TIGRFAMsiTIGR01121. D_amino_aminoT. 1 hit.
    PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P19938-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGYTLWNDQI VKDEEVKIDK EDRGYQFGDG VYEVVKVYNG EMFTVNEHID
    60 70 80 90 100
    RLYASAEKIR ITIPYTKDKF HQLLHELVEK NELNTGHIYF QVTRGTSPRA
    110 120 130 140 150
    HQFPENTVKP VIIGYTKENP RPLENLEKGV KATFVEDIRW LRCDIKSLNL
    160 170 180 190 200
    LGAVLAKQEA HEKGCYEAIL HRNNTVTEGS SSNVFGIKDG ILYTHPANNM
    210 220 230 240 250
    ILKGITRDVV IACANEINMP VKEIPFTTHE ALKMDELFVT STTSEITPVI
    260 270 280
    EIDGKLIRDG KVGEWTRKLQ KQFETKIPKP LHI
    Length:283
    Mass (Da):32,396
    Last modified:January 23, 2007 - v2
    Checksum:i21563BDC35BE98F3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04460 Genomic DNA. Translation: AAA22252.1.
    PIRiA31422.

    Genome annotation databases

    KEGGiag:AAA22252.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J04460 Genomic DNA. Translation: AAA22252.1.
    PIRiA31422.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1A0GX-ray2.00A/B2-283[»]
    1DAAX-ray1.94A/B2-283[»]
    1G2WX-ray2.00A/B2-283[»]
    2DAAX-ray2.10A/B2-283[»]
    2DABX-ray2.00A/B2-283[»]
    3DAAX-ray1.90A/B2-278[»]
    3LQSX-ray1.90A/B2-281[»]
    4DAAX-ray2.40A/B2-278[»]
    5DAAX-ray2.90A/B2-278[»]
    ProteinModelPortaliP19938.
    SMRiP19938.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:AAA22252.

    Phylogenomic databases

    KOiK00824.

    Enzyme and pathway databases

    BRENDAi2.6.1.21. 691.
    SABIO-RKP19938.

    Miscellaneous databases

    EvolutionaryTraceiP19938.

    Family and domain databases

    InterProiIPR001544. Aminotrans_IV.
    IPR018300. Aminotrans_IV_CS.
    IPR005784. D_amino_transT.
    [Graphical view]
    PANTHERiPTHR11825. PTHR11825. 1 hit.
    PfamiPF01063. Aminotran_4. 1 hit.
    [Graphical view]
    SUPFAMiSSF56752. SSF56752. 1 hit.
    TIGRFAMsiTIGR01121. D_amino_aminoT. 1 hit.
    PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDAAA_BACYM
    AccessioniPrimary (citable) accession number: P19938
    Secondary accession number(s): P83771
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: January 23, 2007
    Last modified: November 2, 2016
    This is version 101 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. 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.