ID BAUA_PSEAE Reviewed; 448 AA. AC Q9I700; DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 117. DE RecName: Full=Beta-alanine--pyruvate aminotransferase; DE Short=Beta-A--Py AT; DE EC=2.6.1.18; DE AltName: Full=Beta-alanine--pyruvate transaminase; DE AltName: Full=Omega-amino acid aminotransferase; DE Short=Omega-amino acid AT; DE AltName: Full=Omega-amino acid--pyruvate aminotransferase; DE Short=Omega-APT; GN Name=bauA; OrderedLocusNames=PA0132; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). RN [2] RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=21622750; DOI=10.1128/jb.05105-11; RA Yao X., He W., Lu C.D.; RT "Functional characterization of seven gamma-glutamylpolyamine synthetase RT genes and the bauRABCD locus for polyamine and beta-alanine utilization in RT Pseudomonas aeruginosa PAO1."; RL J. Bacteriol. 193:3923-3930(2011). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND RP PYRIDOXAL PHOSPHATE, FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBSTRATE RP SPECIFICITY, AND SUBUNIT. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=23519665; DOI=10.1107/s0907444912051670; RA Sayer C., Isupov M.N., Westlake A., Littlechild J.A.; RT "Structural studies of Pseudomonas and Chromobacterium omega- RT aminotransferases provide insights into their differing substrate RT specificity."; RL Acta Crystallogr. D 69:564-576(2013). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, RP COFACTOR, AND SUBUNIT. RA Lebedev A.A., Isupov M.N.; RT "Space group and origin ambiguity in structures with pseudosymmetry and RT their treatment in program zanuda."; RL Submitted (MAY-2013) to the PDB data bank. CC -!- FUNCTION: Involved in the degradation of beta-alanine. Catalyzes the CC transfer of the amino group from beta-alanine to pyruvate to yield L- CC alanine and 3-oxopropanoate. It can also accept both 4-aminobutyrate CC and (S)-alpha-methylbenzylamine (MBA) as amino-group donors in the CC presence of pyruvate as an amine acceptor. CC {ECO:0000269|PubMed:21622750, ECO:0000269|PubMed:23519665}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3-oxopropanoate + L-alanine = beta-alanine + pyruvate; CC Xref=Rhea:RHEA:14077, ChEBI:CHEBI:15361, ChEBI:CHEBI:33190, CC ChEBI:CHEBI:57966, ChEBI:CHEBI:57972; EC=2.6.1.18; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:23519665, ECO:0000269|Ref.4}; CC -!- ACTIVITY REGULATION: Inhibited by gabaculine (5-amino-1,3- CC cyclohexadienylcarboxylic acid). {ECO:0000269|PubMed:23519665}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23519665, CC ECO:0000269|Ref.4}. CC -!- INDUCTION: Activated by BauR. {ECO:0000269|PubMed:21622750}. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow normally on CC putrescine, cadaverine, and GABA, but growth on beta-alanine is CC completely abolished. {ECO:0000269|PubMed:21622750}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004091; AAG03522.1; -; Genomic_DNA. DR PIR; F83628; F83628. DR RefSeq; NP_248822.1; NC_002516.2. DR RefSeq; WP_003083801.1; NZ_QZGE01000015.1. DR PDB; 4B98; X-ray; 1.65 A; A/B/C/D=1-448. DR PDB; 4B9B; X-ray; 1.64 A; A/B/C/D/E/F/G/H=1-448. DR PDB; 4BQ0; X-ray; 1.77 A; A/B/C/D=1-448. DR PDBsum; 4B98; -. DR PDBsum; 4B9B; -. DR PDBsum; 4BQ0; -. DR AlphaFoldDB; Q9I700; -. DR SMR; Q9I700; -. DR STRING; 208964.PA0132; -. DR PaxDb; 208964-PA0132; -. DR GeneID; 879350; -. DR KEGG; pae:PA0132; -. DR PATRIC; fig|208964.12.peg.137; -. DR PseudoCAP; PA0132; -. DR HOGENOM; CLU_016922_4_3_6; -. DR InParanoid; Q9I700; -. DR OrthoDB; 9801052at2; -. DR PhylomeDB; Q9I700; -. DR BioCyc; PAER208964:G1FZ6-134-MONOMER; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central. DR GO; GO:0016223; F:beta-alanine-pyruvate transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0019483; P:beta-alanine biosynthetic process; IDA:PseudoCAP. DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central. DR CDD; cd00610; OAT_like; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1. DR PANTHER; PTHR42684:SF1; BETA-ALANINE--PYRUVATE AMINOTRANSFERASE; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminotransferase; Pyridoxal phosphate; Pyruvate; KW Reference proteome; Transferase. FT CHAIN 1..448 FT /note="Beta-alanine--pyruvate aminotransferase" FT /id="PRO_0000428971" FT BINDING 61 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23519665" FT BINDING 120..121 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT BINDING 327 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT /evidence="ECO:0000269|PubMed:23519665, ECO:0000269|Ref.4" FT BINDING 414 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23519665" FT BINDING 421 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:23519665" FT MOD_RES 288 FT /note="N6-(pyridoxal phosphate)lysine" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:4B98" FT HELIX 17..19 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 27..32 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 36..42 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 52..55 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 58..61 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 70..82 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 94..105 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 111..119 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 120..137 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 145..149 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 158..163 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 167..170 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 201..205 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 207..215 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 220..225 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:4B9B" FT TURN 230..233 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 241..252 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 255..259 FT /evidence="ECO:0007829|PDB:4B9B" FT TURN 261..268 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 269..271 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 273..277 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 282..286 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 288..291 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 298..303 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 304..311 FT /evidence="ECO:0007829|PDB:4B9B" FT TURN 327..330 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 332..347 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 350..366 FT /evidence="ECO:0007829|PDB:4B9B" FT TURN 367..370 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 374..380 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 383..388 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 397..408 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 414..416 FT /evidence="ECO:0007829|PDB:4B9B" FT STRAND 419..422 FT /evidence="ECO:0007829|PDB:4B9B" FT HELIX 430..445 FT /evidence="ECO:0007829|PDB:4B9B" SQ SEQUENCE 448 AA; 48382 MW; BEC87B105289BD1E CRC64; MNQPLNVAPP VSSELNLRAH WMPFSANRNF QKDPRIIVAA EGSWLTDDKG RKVYDSLSGL WTCGAGHSRK EIQEAVARQL GTLDYSPGFQ YGHPLSFQLA EKIAGLLPGE LNHVFFTGSG SECADTSIKM ARAYWRLKGQ PQKTKLIGRA RGYHGVNVAG TSLGGIGGNR KMFGQLMDVD HLPHTLQPGM AFTRGMAQTG GVELANELLK LIELHDASNI AAVIVEPMSG SAGVLVPPVG YLQRLREICD QHNILLIFDE VITAFGRLGT YSGAEYFGVT PDLMNVAKQV TNGAVPMGAV IASSEIYDTF MNQALPEHAV EFSHGYTYSA HPVACAAGLA ALDILARDNL VQQSAELAPH FEKGLHGLQG AKNVIDIRNC GLAGAIQIAP RDGDPTVRPF EAGMKLWQQG FYVRFGGDTL QFGPTFNARP EELDRLFDAV GEALNGIA //