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Q9I700

- BAUA_PSEAE

UniProt

Q9I700 - BAUA_PSEAE

Protein

Beta-alanine--pyruvate aminotransferase

Gene

bauA

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
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    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 – 611Substrate1 Publication
    Binding sitei327 – 3271Pyridoxal phosphate2 Publications
    Binding sitei414 – 4141Substrate1 Publication
    Binding sitei421 – 4211Substrate1 Publication

    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

    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.1 Publication

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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: October 1, 2014
    This is version 74 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