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P19938 (DAAA_BACYM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:dat
OrganismBacillus sp. (strain YM-1)
Taxonomic identifier72579 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.4

Catalytic activity

D-alanine + 2-oxoglutarate = pyruvate + D-glutamate. Ref.2 Ref.4

Cofactor

Pyridoxal phosphate. Ref.3

Subunit structure

Homodimer. Ref.2 Ref.3

Sequence similarities

Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.

Biophysicochemical properties

Absorption:

Abs(max)=279 nm Ref.2

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.

Kinetic parameters:

KM=2.2 mM for D-alanine

KM=5.9 mM for alpha-ketoglutarate

KM=2.2 mM for alpha-ketobutyrate

KM=2.2 mM for alpha-ketovalerate

pH dependence:

Optimum pH is 8.3.

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 283282D-alanine aminotransferase
PRO_0000103248

Sites

Active site1461Proton acceptor
Binding site321Substrate
Binding site511Pyridoxal phosphate
Binding site991Substrate
Binding site1011Substrate
Binding site1781Pyridoxal phosphate
Binding site2021Pyridoxal phosphate

Amino acid modifications

Modified residue1461N6-(pyridoxal phosphate)lysine

Experimental info

Mutagenesis1781E → K: Loss of transaminase activity and small gain in racemase activity. Ref.6
Mutagenesis2021L → A: Inactivates enzyme. Ref.5

Secondary structure

.............................................. 283
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19938 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 21563BDC35BE98F3

FASTA28332,396
        10         20         30         40         50         60 
MGYTLWNDQI VKDEEVKIDK EDRGYQFGDG VYEVVKVYNG EMFTVNEHID RLYASAEKIR 

        70         80         90        100        110        120 
ITIPYTKDKF HQLLHELVEK NELNTGHIYF QVTRGTSPRA HQFPENTVKP VIIGYTKENP 

       130        140        150        160        170        180 
RPLENLEKGV KATFVEDIRW LRCDIKSLNL LGAVLAKQEA HEKGCYEAIL HRNNTVTEGS 

       190        200        210        220        230        240 
SSNVFGIKDG ILYTHPANNM ILKGITRDVV IACANEINMP VKEIPFTTHE ALKMDELFVT 

       250        260        270        280 
STTSEITPVI EIDGKLIRDG KVGEWTRKLQ KQFETKIPKP LHI 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04460 Genomic DNA. Translation: AAA22252.1.
PIRA31422.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A0GX-ray2.00A/B2-283[»]
1DAAX-ray1.94A/B2-283[»]
1G2WX-ray2.00A/B2-283[»]
2DAAX-ray2.10A/B2-282[»]
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[»]
ProteinModelPortalP19938.
SMRP19938. Positions 2-278.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP19938.

Family and domain databases

InterProIPR001544. Aminotrans_IV.
IPR018300. Aminotrans_IV_CS.
IPR005784. D_amino_transT.
[Graphical view]
PANTHERPTHR11825. PTHR11825. 1 hit.
PfamPF01063. Aminotran_4. 1 hit.
[Graphical view]
SUPFAMSSF56752. SSF56752. 1 hit.
TIGRFAMsTIGR01121. D_amino_aminoT. 1 hit.
PROSITEPS00770. AA_TRANSFER_CLASS_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP19938.

Entry information

Entry nameDAAA_BACYM
AccessionPrimary (citable) accession number: P19938
Secondary accession number(s): P83771
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: October 16, 2013
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references