ID   BAUC_PSEAE              Reviewed;         497 AA.
AC   Q9I702;
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=Putative 3-oxopropanoate dehydrogenase;
DE            EC=1.2.1.-;
GN   Name=bauC; OrderedLocusNames=PA0130;
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.
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).
CC   -!- FUNCTION: Involved in the degradation of beta-alanine.
CC       {ECO:0000269|PubMed:21622750}.
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 aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AE004091; AAG03520.1; -; Genomic_DNA.
DR   PIR; D83628; D83628.
DR   RefSeq; NP_248820.1; NC_002516.2.
DR   RefSeq; WP_003101230.1; NZ_QZGE01000015.1.
DR   AlphaFoldDB; Q9I702; -.
DR   SMR; Q9I702; -.
DR   STRING; 287.DR97_3087; -.
DR   PaxDb; Q9I702; -.
DR   PRIDE; Q9I702; -.
DR   EnsemblBacteria; AAG03520; AAG03520; PA0130.
DR   GeneID; 880875; -.
DR   KEGG; pae:PA0130; -.
DR   PATRIC; fig|208964.12.peg.135; -.
DR   PseudoCAP; PA0130; -.
DR   HOGENOM; CLU_005391_1_10_6; -.
DR   InParanoid; Q9I702; -.
DR   OMA; YPLAIVC; -.
DR   PhylomeDB; Q9I702; -.
DR   BioCyc; PAER208964:G1FZ6-132-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; IBA:GO_Central.
DR   GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IBA:GO_Central.
DR   GO; GO:0019483; P:beta-alanine biosynthetic process; IDA:PseudoCAP.
DR   GO; GO:0006210; P:thymine catabolic process; IBA:GO_Central.
DR   GO; GO:0006574; P:valine catabolic process; IBA:GO_Central.
DR   CDD; cd07085; ALDH_F6_MMSDH; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR010061; MeMal-semiAld_DH.
DR   PANTHER; PTHR43866; PTHR43866; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01722; MMSDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Putative 3-oxopropanoate dehydrogenase"
FT                   /id="PRO_0000428972"
FT   ACT_SITE        280
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         224..229
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  53323 MW;  013A59DF1039AD7A CRC64;
     MGTLHHLING EMVADNGRSA DVFNPSTGEA IHKVPLADGK TLQKAIDAAR AAFPAWRNTP
     PAKRAQVLYR FKQLLEQNEA RISKLISEEH GKTLEDAAGE LKRGIENVEY ACAAPEILKG
     EYSRNVGPNI DAWSDFQPIG VVAGITPFNF PAMVPLWMYP LAIACGNTFI LKPSERDPSS
     TLLIAELFHE AGLPKGVLNV VHGDKEAVDG LLQAPEVKAI SFVGSTPIAE YIYAEGTKRG
     KRVQALGGAK NHAVLMPDAD LDNAVSALMG AAYGSCGERC MAISVAVCVG DQVADALIAK
     LVPQIKALKI GAGTSCGLDM GPLVTAAAQA KVTGYIDSGV AQGAELVVDG RGYQVAGHEN
     GFFLGGSLFD RVTPEMTIYK EEIFGPVLCV VRVNSLEEAM QLINDHEYGN GTCIFTRDGE
     AARLFCDEIE VGMVGVNVPL PVPVAYHSFG GWKRSLFGDL HAYGPDGVRF YTRRKAITQR
     WPQRASHEAS QFAFPSL