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P19938

- DAAA_BACYM

UniProt

P19938 - DAAA_BACYM

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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

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-alanine
  2. KM=5.9 mM for alpha-ketoglutarate
  3. KM=2.2 mM for alpha-ketobutyrate
  4. KM=2.2 mM for alpha-ketovalerate

pH dependencei

Optimum pH is 8.3.

Temperature dependencei

Optimum temperature is 60 degrees Celsius.

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
Complete GO annotation...

GO - Biological processi

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

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

SABIO-RKiP19938.

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 aminotransferase
PRO_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

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.

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...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RKi 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: July 9, 2014
This is version 91 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

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