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P19938

- DAAA_BACYM

UniProt

P19938 - DAAA_BACYM

Protein

D-alanine aminotransferase

Gene

dat

Organism
Bacillus sp. (strain YM-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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 phosphate.1 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei32 – 321Substrate
    Binding sitei51 – 511Pyridoxal phosphate
    Binding sitei99 – 991Substrate
    Binding sitei101 – 1011Substrate
    Active sitei146 – 1461Proton acceptor
    Binding sitei178 – 1781Pyridoxal phosphate
    Binding sitei202 – 2021Pyridoxal phosphate

    GO - Molecular functioni

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

    GO - Biological processi

    1. D-amino acid biosynthetic process Source: UniProtKB
    2. D-amino acid catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi178 – 1781E → K: Loss of transaminase activity and small gain in racemase activity. 1 Publication
    Mutagenesisi202 – 2021L → A: Inactivates enzyme. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 283282D-alanine aminotransferasePRO_0000103248Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei146 – 1461N6-(pyridoxal phosphate)lysine

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Beta strandi9 – 124
    Helixi13 – 153
    Helixi23 – 264
    Beta strandi30 – 389
    Beta strandi41 – 444
    Helixi45 – 5814
    Helixi67 – 8115
    Beta strandi85 – 9410
    Beta strandi111 – 1188
    Helixi123 – 1286
    Beta strandi130 – 1367
    Helixi151 – 16212
    Beta strandi166 – 1727
    Beta strandi175 – 1795
    Beta strandi182 – 1887
    Beta strandi191 – 1944
    Helixi205 – 21612
    Helixi228 – 2325
    Beta strandi235 – 2417
    Turni242 – 2443
    Beta strandi245 – 2528
    Beta strandi255 – 2573
    Turni258 – 2603
    Helixi264 – 27411

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-278.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19938.

    Family & Domainsi

    Sequence similaritiesi

    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

    MGYTLWNDQI VKDEEVKIDK EDRGYQFGDG VYEVVKVYNG EMFTVNEHID    50
    RLYASAEKIR ITIPYTKDKF HQLLHELVEK NELNTGHIYF QVTRGTSPRA 100
    HQFPENTVKP VIIGYTKENP RPLENLEKGV KATFVEDIRW LRCDIKSLNL 150
    LGAVLAKQEA HEKGCYEAIL HRNNTVTEGS SSNVFGIKDG ILYTHPANNM 200
    ILKGITRDVV IACANEINMP VKEIPFTTHE ALKMDELFVT STTSEITPVI 250
    EIDGKLIRDG KVGEWTRKLQ KQFETKIPKP LHI 283
    Length:283
    Mass (Da):32,396
    Last modified:January 23, 2007 - v2
    Checksum:i21563BDC35BE98F3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04460 Genomic DNA. Translation: AAA22252.1.
    PIRiA31422.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04460 Genomic DNA. Translation: AAA22252.1 .
    PIRi A31422.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A0G X-ray 2.00 A/B 2-283 [» ]
    1DAA X-ray 1.94 A/B 2-283 [» ]
    1G2W X-ray 2.00 A/B 2-283 [» ]
    2DAA X-ray 2.10 A/B 2-283 [» ]
    2DAB X-ray 2.00 A/B 2-283 [» ]
    3DAA X-ray 1.90 A/B 2-278 [» ]
    3LQS X-ray 1.90 A/B 2-281 [» ]
    4DAA X-ray 2.40 A/B 2-278 [» ]
    5DAA X-ray 2.90 A/B 2-278 [» ]
    ProteinModelPortali P19938.
    SMRi P19938. Positions 2-278.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P19938.

    Miscellaneous databases

    EvolutionaryTracei P19938.

    Family and domain databases

    InterProi IPR001544. Aminotrans_IV.
    IPR018300. Aminotrans_IV_CS.
    IPR005784. D_amino_transT.
    [Graphical view ]
    PANTHERi PTHR11825. PTHR11825. 1 hit.
    Pfami PF01063. Aminotran_4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56752. SSF56752. 1 hit.
    TIGRFAMsi TIGR01121. D_amino_aminoT. 1 hit.
    PROSITEi PS00770. AA_TRANSFER_CLASS_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases."
      Tanizawa K., Asano S., Masu Y., Kuramitsu S., Kagamiyama H., Tanaka H., Soda K.
      J. Biol. Chem. 264:2450-2454(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. "Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination."
      Tanizawa K., Masu Y., Asano S., Tanaka H., Soda K.
      J. Biol. Chem. 264:2445-2449(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21; 143-157 AND 281-283, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    3. "Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity."
      Sugio S., Petsko G.A., Manning J.M., Soda K., Ringe D.
      Biochemistry 34:9661-9669(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS), COFACTOR, SUBUNIT.
    4. "Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase."
      Peisach D., Chipman D.M., van Ophem P.W., Manning J.M., Petsko G.A., Ringe D.
      Biochemistry 37:4958-4967(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY.
    5. "Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0-A resolution: implication of the structural role of Leu201 in transamination."
      Sugio S., Kashima A., Kishimoto K., Peisach D., Petsko G.A., Ringe D., Yoshimura T., Esaki N.
      Protein Eng. 11:613-619(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), MUTAGENESIS OF LEU-202.
    6. "Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity."
      van Ophem P.W., Peisach D., Erickson S.D., Soda K., Ringe D., Manning J.M.
      Biochemistry 38:1323-1331(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), MUTAGENESIS OF GLU-178.

    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: October 1, 2014
    This is version 92 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

    External Data

    Dasty 3