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Q9I700

- BAUA_PSEAE

UniProt

Q9I700 - BAUA_PSEAE

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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

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 5'-phosphate2 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
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.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 – 143Combined sources
Helixi17 – 193Combined sources
Helixi27 – 326Combined sources
Beta strandi36 – 427Combined sources
Beta strandi44 – 474Combined sources
Beta strandi52 – 554Combined sources
Helixi58 – 614Combined sources
Helixi70 – 8213Combined sources
Beta strandi88 – 903Combined sources
Helixi94 – 10512Combined sources
Beta strandi111 – 1199Combined sources
Helixi120 – 13718Combined sources
Beta strandi145 – 1495Combined sources
Helixi158 – 1636Combined sources
Helixi167 – 1704Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi198 – 2003Combined sources
Helixi201 – 2055Combined sources
Helixi207 – 2159Combined sources
Helixi217 – 2193Combined sources
Beta strandi220 – 2256Combined sources
Beta strandi227 – 2293Combined sources
Turni230 – 2334Combined sources
Helixi241 – 25212Combined sources
Beta strandi255 – 2595Combined sources
Turni261 – 2688Combined sources
Beta strandi269 – 2713Combined sources
Helixi273 – 2775Combined sources
Beta strandi282 – 2865Combined sources
Helixi288 – 2914Combined sources
Beta strandi298 – 3036Combined sources
Helixi304 – 3118Combined sources
Turni327 – 3304Combined sources
Helixi332 – 34716Combined sources
Helixi350 – 36617Combined sources
Turni367 – 3704Combined sources
Beta strandi374 – 3807Combined sources
Beta strandi383 – 3886Combined sources
Helixi397 – 40812Combined sources
Beta strandi414 – 4163Combined sources
Beta strandi419 – 4224Combined sources
Helixi430 – 44516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

InParanoidiQ9I700.
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

        10         20         30         40         50
MNQPLNVAPP VSSELNLRAH WMPFSANRNF QKDPRIIVAA EGSWLTDDKG
60 70 80 90 100
RKVYDSLSGL WTCGAGHSRK EIQEAVARQL GTLDYSPGFQ YGHPLSFQLA
110 120 130 140 150
EKIAGLLPGE LNHVFFTGSG SECADTSIKM ARAYWRLKGQ PQKTKLIGRA
160 170 180 190 200
RGYHGVNVAG TSLGGIGGNR KMFGQLMDVD HLPHTLQPGM AFTRGMAQTG
210 220 230 240 250
GVELANELLK LIELHDASNI AAVIVEPMSG SAGVLVPPVG YLQRLREICD
260 270 280 290 300
QHNILLIFDE VITAFGRLGT YSGAEYFGVT PDLMNVAKQV TNGAVPMGAV
310 320 330 340 350
IASSEIYDTF MNQALPEHAV EFSHGYTYSA HPVACAAGLA ALDILARDNL
360 370 380 390 400
VQQSAELAPH FEKGLHGLQG AKNVIDIRNC GLAGAIQIAP RDGDPTVRPF
410 420 430 440
EAGMKLWQQG FYVRFGGDTL QFGPTFNARP EELDRLFDAV GEALNGIA
Length:448
Mass (Da):48,382
Last modified:March 1, 2001 - v1
Checksum:iBEC87B105289BD1E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AE004091 Genomic DNA. Translation: AAG03522.1 .
PIRi F83628.
RefSeqi NP_248822.1. NC_002516.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

InParanoidi Q9I700.
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: November 26, 2014
This is version 76 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