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Q9I700

- BAUA_PSEAE

UniProt

Q9I700 - BAUA_PSEAE

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Protein

Beta-alanine--pyruvate aminotransferase

Gene
bauA, PA0132
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Cofactori

Pyridoxal phosphate.2 Publications

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei61 – 611Substrate
Binding sitei327 – 3271Pyridoxal phosphate
Binding sitei414 – 4141Substrate
Binding sitei421 – 4211Substrate

GO - Molecular functioni

  1. beta-alanine-pyruvate transaminase activity Source: UniProtKB-EC
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. beta-alanine biosynthetic process Source: PseudoCAP
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate, Pyruvate

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-alanine--pyruvate aminotransferase (EC:2.6.1.18)
Short name:
Beta-A--Py AT
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 namesi
Name:bauA
Ordered Locus Names:PA0132
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438: Chromosome

Organism-specific databases

PseudoCAPiPA0132.

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene grow normally on putrescine, cadaverine, and GABA, but growth on beta-alanine is completely abolished.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 448448Beta-alanine--pyruvate aminotransferasePRO_0000428971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei288 – 2881N6-(pyridoxal phosphate)lysine

Expressioni

Inductioni

Activated by BauR.2 Publications

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

STRINGi208964.PA0132.

Structurei

Secondary structure

1
448
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi12 – 143
Helixi17 – 193
Helixi27 – 326
Beta strandi36 – 427
Beta strandi44 – 474
Beta strandi52 – 554
Helixi58 – 614
Helixi70 – 8213
Beta strandi88 – 903
Helixi94 – 10512
Beta strandi111 – 1199
Helixi120 – 13718
Beta strandi145 – 1495
Helixi158 – 1636
Helixi167 – 1704
Beta strandi180 – 1823
Beta strandi198 – 2003
Helixi201 – 2055
Helixi207 – 2159
Helixi217 – 2193
Beta strandi220 – 2256
Beta strandi227 – 2293
Turni230 – 2334
Helixi241 – 25212
Beta strandi255 – 2595
Turni261 – 2688
Beta strandi269 – 2713
Helixi273 – 2775
Beta strandi282 – 2865
Helixi288 – 2914
Beta strandi298 – 3036
Helixi304 – 3118
Turni327 – 3304
Helixi332 – 34716
Helixi350 – 36617
Turni367 – 3704
Beta strandi374 – 3807
Beta strandi383 – 3886
Helixi397 – 40812
Beta strandi414 – 4163
Beta strandi419 – 4224
Helixi430 – 44516

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9I700.
SMRiQ9I700. Positions 13-448.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 1212Pyridoxal phosphate binding

Sequence similaritiesi

Phylogenomic databases

KOiK00822.
OMAiDYMLEFP.
OrthoDBiEOG6W71WN.
PhylomeDBiQ9I700.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProiIPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERiPTHR11986. PTHR11986. 1 hit.
PfamiPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9I700-1 [UniParc]FASTAAdd to Basket

« Hide

MNQPLNVAPP VSSELNLRAH WMPFSANRNF QKDPRIIVAA EGSWLTDDKG    50
RKVYDSLSGL WTCGAGHSRK EIQEAVARQL GTLDYSPGFQ YGHPLSFQLA 100
EKIAGLLPGE LNHVFFTGSG SECADTSIKM ARAYWRLKGQ PQKTKLIGRA 150
RGYHGVNVAG TSLGGIGGNR KMFGQLMDVD HLPHTLQPGM AFTRGMAQTG 200
GVELANELLK LIELHDASNI AAVIVEPMSG SAGVLVPPVG YLQRLREICD 250
QHNILLIFDE VITAFGRLGT YSGAEYFGVT PDLMNVAKQV TNGAVPMGAV 300
IASSEIYDTF MNQALPEHAV EFSHGYTYSA HPVACAAGLA ALDILARDNL 350
VQQSAELAPH FEKGLHGLQG AKNVIDIRNC GLAGAIQIAP RDGDPTVRPF 400
EAGMKLWQQG FYVRFGGDTL QFGPTFNARP EELDRLFDAV GEALNGIA 448
Length:448
Mass (Da):48,382
Last modified:March 1, 2001 - v1
Checksum:iBEC87B105289BD1E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG03522.1.
PIRiF83628.
RefSeqiNP_248822.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG03522; AAG03522; PA0132.
GeneIDi879350.
KEGGipae:PA0132.
PATRICi19834470. VBIPseAer58763_0137.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004091 Genomic DNA. Translation: AAG03522.1 .
PIRi F83628.
RefSeqi NP_248822.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4B98 X-ray 1.65 A/B/C/D 1-448 [» ]
4B9B X-ray 1.64 A/B/C/D/E/F/G/H 1-448 [» ]
4BQ0 X-ray 1.77 A/B/C/D 1-448 [» ]
ProteinModelPortali Q9I700.
SMRi Q9I700. Positions 13-448.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA0132.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG03522 ; AAG03522 ; PA0132 .
GeneIDi 879350.
KEGGi pae:PA0132.
PATRICi 19834470. VBIPseAer58763_0137.

Organism-specific databases

PseudoCAPi PA0132.

Phylogenomic databases

KOi K00822.
OMAi DYMLEFP.
OrthoDBi EOG6W71WN.
PhylomeDBi Q9I700.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProi IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
PANTHERi PTHR11986. PTHR11986. 1 hit.
Pfami PF00202. Aminotran_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMi SSF53383. SSF53383. 1 hit.
PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiBAUA_PSEAE
AccessioniPrimary (citable) accession number: Q9I700
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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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