FEAB_ECOLI
ID FEAB_ECOLI Reviewed; 499 AA.
AC P80668; O32557; P46884; P77637;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Phenylacetaldehyde dehydrogenase;
DE Short=PAD;
DE EC=1.2.1.39;
GN Name=feaB; Synonyms=maoB, padA, ydbG; OrderedLocusNames=b1385, JW1380;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-9.
RC STRAIN=K12;
RX PubMed=9043126; DOI=10.1099/00221287-143-2-513;
RA Hanlon S.P., Hill T.K., Flavell M.A., Stringfellow J.M., Cooper R.A.;
RT "2-phenylethylamine catabolism by Escherichia coli K-12: gene organization
RT and expression.";
RL Microbiology 143:513-518(1997).
RN [2]
RP SEQUENCE REVISION.
RA Stringfellow J.M.;
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=W / ATCC 11105 / DSM 1900;
RX PubMed=9109378; DOI=10.1016/s0014-5793(97)00228-7;
RA Ferrandez A., Prieto M.A., Garcia J.L., Diaz E.;
RT "Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase
RT from Escherichia coli.";
RL FEBS Lett. 406:23-27(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Azakami H., Yamashita M., Roh J.-H., Suzuki H., Kumagai H., Murooka Y.;
RT "Nucleotide sequence of the gene for monoamine oxidase (maoA) from
RT Escherichia coli.";
RL J. Ferment. Bioeng. 77:315-319(1994).
CC -!- FUNCTION: Acts almost equally well on phenylacetaldehyde, 4-
CC hydroxyphenylacetaldehyde and 3,4-dihydroxyphenylacetaldehyde.
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 -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC phenylacetate from L-phenylalanine: step 3/3.
CC -!- SUBUNIT: Homodimer.
CC -!- MISCELLANEOUS: Can also use NADP, but prefers NAD.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X99402; CAA67780.1; -; Genomic_DNA.
DR EMBL; X97453; CAA66106.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74467.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA14992.2; -; Genomic_DNA.
DR EMBL; D23670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D64889; D64889.
DR RefSeq; NP_415903.4; NC_000913.3.
DR RefSeq; WP_000138615.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P80668; -.
DR SMR; P80668; -.
DR BioGRID; 4261813; 11.
DR DIP; DIP-9581N; -.
DR IntAct; P80668; 1.
DR STRING; 511145.b1385; -.
DR jPOST; P80668; -.
DR PaxDb; P80668; -.
DR PRIDE; P80668; -.
DR EnsemblBacteria; AAC74467; AAC74467; b1385.
DR EnsemblBacteria; BAA14992; BAA14992; BAA14992.
DR GeneID; 945933; -.
DR KEGG; ecj:JW1380; -.
DR KEGG; eco:b1385; -.
DR PATRIC; fig|1411691.4.peg.887; -.
DR EchoBASE; EB2971; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_0_2_6; -.
DR InParanoid; P80668; -.
DR OMA; DADMGHA; -.
DR PhylomeDB; P80668; -.
DR BioCyc; EcoCyc:PHENDEHYD-MON; -.
DR BioCyc; MetaCyc:PHENDEHYD-MON; -.
DR BRENDA; 1.2.1.39; 2026.
DR UniPathway; UPA00139; UER00724.
DR PRO; PR:P80668; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0047106; F:4-hydroxyphenylacetaldehyde dehydrogenase activity; IDA:EcoliWiki.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:EcoliWiki.
DR GO; GO:0008957; F:phenylacetaldehyde dehydrogenase activity; IDA:EcoCyc.
DR GO; GO:0046196; P:4-nitrophenol catabolic process; IDA:EcoliWiki.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:EcoliWiki.
DR GO; GO:0019607; P:phenylethylamine catabolic process; IDA:EcoCyc.
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 Direct protein sequencing; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..499
FT /note="Phenylacetaldehyde dehydrogenase"
FT /id="PRO_0000056575"
FT ACT_SITE 272
FT /evidence="ECO:0000250"
FT ACT_SITE 306
FT /evidence="ECO:0000250"
FT BINDING 250..255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 265
FT /note="H -> R (in Ref. 3; CAA66106)"
FT /evidence="ECO:0000305"
FT CONFLICT 484..499
FT /note="DWLDGWCETKSVCVRY -> PLAGRAGC (in Ref. 1; CAA67780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 53699 MW; 18D7C7D1BE136464 CRC64;
MTEPHVAVLS QVQQFLDRQH GLYIDGRPGP AQSEKRLAIF DPATGQEIAS TADANEADVD
NAVMSAWRAF VSRRWAGRLP AERERILLRF ADLVEQHSEE LAQLETLEQG KSIAISRAFE
VGCTLNWMRY TAGLTTKIAG KTLDLSIPLP QGARYQAWTR KEPVGVVAGI VPWNFPLMIG
MWKVMPALAA GCSIVIKPSE TTPLTMLRVA ELASEAGIPD GVFNVVTGSG AVCGAALTSH
PHVAKISFTG STATGKGIAR TAADHLTRVT LELGGKNPAI VLKDADPQWV IEGLMTGSFL
NQGQVCAASS RIYIEAPLFD TLVSGFEQAV KSLQVGPGMS PVAQINPLVS RAHCDKVCSF
LDDAQAQQAE LIRGSNGPAG EGYYVAPTLV VNPDAKLRLT REEVFGPVVN LVRVADGEEA
LQLANDTEYG LTASVWTQNL SQALEYSDRL QAGTVWVNSH TLIDANLPFG GMKQSGTGRD
FGPDWLDGWC ETKSVCVRY
