BAUA_PSEAE
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 03-AUG-2022, entry version 109.
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; Proteobacteria; 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 / 1C /
RC 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 / 1C /
RC 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 / 1C /
RC 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; 287.DR97_3089; -.
DR PaxDb; Q9I700; -.
DR PRIDE; Q9I700; -.
DR EnsemblBacteria; AAG03522; AAG03522; 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 OMA; YHGVNIA; -.
DR PhylomeDB; Q9I700; -.
DR BioCyc; PAER208964:G1FZ6-134-MON; -.
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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 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
