ID   STYD_PSEFL              Reviewed;         502 AA.
AC   O06837;
DT   01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Phenylacetaldehyde dehydrogenase;
DE            Short=PAD;
DE            EC=1.2.1.39;
GN   Name=styD;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   PATHWAY.
RC   STRAIN=ST;
RX   PubMed=9172343; DOI=10.1128/aem.63.6.2232-2239.1997;
RA   Beltrametti F., Marconi A.M., Bestetti G., Colombo C., Galli E., Ruzzi M.,
RA   Zennaro E.;
RT   "Sequencing and functional analysis of styrene catabolism genes from
RT   Pseudomonas fluorescens ST.";
RL   Appl. Environ. Microbiol. 63:2232-2239(1997).
CC   -!- FUNCTION: Phenylacetaldehyde dehydrogenase that catalyzes the last step
CC       in the aerobic styrene degradation pathway by mediating oxidation of
CC       phenylacetaldehyde to phenylacetic acid. {ECO:0000269|PubMed:9172343}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-phenylacetaldehyde + H2O + NAD(+) = 2-phenylacetate + 2 H(+)
CC         + NADH; Xref=Rhea:RHEA:21392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16424, ChEBI:CHEBI:18401, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.39;
CC         Evidence={ECO:0000269|PubMed:9172343};
CC   -!- PATHWAY: Aromatic compound metabolism. {ECO:0000269|PubMed:9172343}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {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; Z92524; CAB06826.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06837; -.
DR   SMR; O06837; -.
DR   BioCyc; MetaCyc:MON-16949; -.
DR   GO; GO:0008957; F:phenylacetaldehyde dehydrogenase activity; IDA:UniProtKB.
DR   GO; GO:0042207; P:styrene catabolic process; IDA:UniProtKB.
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; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..502
FT                   /note="Phenylacetaldehyde dehydrogenase"
FT                   /id="PRO_0000430452"
FT   ACT_SITE        273
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        307
FT                   /evidence="ECO:0000250"
FT   BINDING         251..256
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   502 AA;  53497 MW;  AA42C5036309D827 CRC64;
     MTRSLTMNSS LPAIDGLRLP HQMLIGGQWV NAQSDKTLNV YNPATGDTLT DVPDGDVEDV
     NAAVESAAAT LQSDAWRRMP PSARERILLR LADLLEAHGD ELARLETLNN GKLLIYSKMM
     EVGASAQWLR YMAGWATKLT GSTLDLSLPL PPDVRSRAST QRVPVGVVAA IIPWNFPLLM
     AVWKIAPALA CGNTVVLKPA EETPLTALRL AELAMEAGLP AGALNVVTGR GETAGDALVR
     HPKVAKVAFT GSTEVGRIIG SACGRSLKAV SLELGGKSPV IVLADCDPQE AAEGAAAAIF
     FNHGQVCTAG SRLYVHESIY EDVIQRLAVI GESIVVGSGL EQGVHMGPMV SKKHHENVLR
     HIRNGIEDGA DLICGGTEAP CAQGFFVKPT IFANREKKDI RLLSQEVFGP VLVATPFSDI
     AEVVNEANRS VYGLGASIWT NDLSAALRIN DELEAGTVWV NTHNMVDPNL PFGGFKDSGV
     GREHGAAAIE HYTTTRSLVI AY