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Q9I700 (BAUA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. 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:
Beta-alanine--pyruvate aminotransferase

Short name=Beta-A--Py AT
EC=2.6.1.18
Alternative name(s):
Beta-alanine--pyruvate transaminase
Omega-amino acid aminotransferase
Short name=Omega-amino acid AT
Omega-amino acid--pyruvate aminotransferase
Short name=Omega-APT
Gene names
Name:bauA
Ordered Locus Names:PA0132
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the degradation of beta-alanine. Catalyzes the transfer of the amino group from beta-alanine to pyruvate to yield L-alanine and 3-oxopropanoate. It can also accept both 4-aminobutyrate and (S)-alpha-methylbenzylamine (MBA) as amino-group donors in the presence of pyruvate as an amine acceptor. Ref.2 Ref.3

Catalytic activity

L-alanine + 3-oxopropanoate = pyruvate + beta-alanine.

Cofactor

Pyridoxal phosphate. Ref.3 Ref.4

Enzyme regulation

Inhibited by gabaculine (5-amino-1,3-cyclohexadienylcarboxylic acid). Ref.3

Subunit structure

Homotetramer. Ref.3 Ref.4

Induction

Activated by BauR. Ref.2 Ref.3

Disruption phenotype

Cells lacking this gene grow normally on putrescine, cadaverine, and GABA, but growth on beta-alanine is completely abolished. Ref.2

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Beta-alanine--pyruvate aminotransferase
PRO_0000428971

Regions

Region120 – 1212Pyridoxal phosphate binding

Sites

Binding site611Substrate
Binding site3271Pyridoxal phosphate
Binding site4141Substrate
Binding site4211Substrate

Amino acid modifications

Modified residue2881N6-(pyridoxal phosphate)lysine

Secondary structure

.............................................................................. 448
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9I700 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: BEC87B105289BD1E

FASTA44848,382
        10         20         30         40         50         60 
MNQPLNVAPP VSSELNLRAH WMPFSANRNF QKDPRIIVAA EGSWLTDDKG RKVYDSLSGL 

        70         80         90        100        110        120 
WTCGAGHSRK EIQEAVARQL GTLDYSPGFQ YGHPLSFQLA EKIAGLLPGE LNHVFFTGSG 

       130        140        150        160        170        180 
SECADTSIKM ARAYWRLKGQ PQKTKLIGRA RGYHGVNVAG TSLGGIGGNR KMFGQLMDVD 

       190        200        210        220        230        240 
HLPHTLQPGM AFTRGMAQTG GVELANELLK LIELHDASNI AAVIVEPMSG SAGVLVPPVG 

       250        260        270        280        290        300 
YLQRLREICD QHNILLIFDE VITAFGRLGT YSGAEYFGVT PDLMNVAKQV TNGAVPMGAV 

       310        320        330        340        350        360 
IASSEIYDTF MNQALPEHAV EFSHGYTYSA HPVACAAGLA ALDILARDNL VQQSAELAPH 

       370        380        390        400        410        420 
FEKGLHGLQG AKNVIDIRNC GLAGAIQIAP RDGDPTVRPF EAGMKLWQQG FYVRFGGDTL 

       430        440 
QFGPTFNARP EELDRLFDAV GEALNGIA 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Functional characterization of seven gamma-glutamylpolyamine synthetase genes and the bauRABCD locus for polyamine and beta-alanine utilization in Pseudomonas aeruginosa PAO1."
Yao X., He W., Lu C.D.
J. Bacteriol. 193:3923-3930(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, DISRUPTION PHENOTYPE.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]"Structural studies of Pseudomonas and Chromobacterium omega-aminotransferases provide insights into their differing substrate specificity."
Sayer C., Isupov M.N., Westlake A., Littlechild J.A.
Acta Crystallogr. D 69:564-576(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND PYRIDOXAL PHOSPHATE, FUNCTION, COFACTOR, ENZYME REGULATION, SUBSTRATE SPECIFICITY, SUBUNIT.
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[4]"Space group and origin ambiguity in structures with pseudosymmetry and their treatment in program zanuda."
Lebedev A.A., Isupov M.N.
Submitted (MAY-2013) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, COFACTOR, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004091 Genomic DNA. Translation: AAG03522.1.
PIRF83628.
RefSeqNP_248822.1. NC_002516.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4B98X-ray1.65A/B/C/D1-448[»]
4B9BX-ray1.64A/B/C/D/E/F/G/H1-448[»]
4BQ0X-ray1.77A/B/C/D1-448[»]
ProteinModelPortalQ9I700.
SMRQ9I700. Positions 13-448.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING208964.PA0132.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG03522; AAG03522; PA0132.
GeneID879350.
KEGGpae:PA0132.
PATRIC19834470. VBIPseAer58763_0137.

Organism-specific databases

PseudoCAPPA0132.

Phylogenomic databases

KOK00822.
OMADYMLEFP.
OrthoDBEOG6W71WN.
PhylomeDBQ9I700.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBAUA_PSEAE
AccessionPrimary (citable) accession number: Q9I700
Entry history
Integrated into UniProtKB/Swiss-Prot: May 14, 2014
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 73 of the entry and version 1 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