Skip Header

Contribute Send feedback
Read comments (?) or add your own

P80668 (FEAB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenylacetaldehyde dehydrogenase

Short name=PAD
EC=1.2.1.39
Gene names
Name:feaB
Synonyms:maoB, padA, ydbG
Ordered Locus Names:b1385, JW1380
OrganismEscherichia coli (strain K12)
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length499 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts almost equally well on phenylacetaldehyde, 4-hydroxyphenylacetaldehyde and 3,4-dihydroxyphenylacetaldehyde.

Catalytic activity

Phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH.

Pathway

Amino-acid degradation; L-phenylalanine degradation; phenylacetate from L-phenylalanine: step 3/3.

Subunit structure

Homodimer.

Miscellaneous

Can also use NADP, but prefers NAD.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 499499Phenylacetaldehyde dehydrogenase
PRO_0000056575

Regions

Nucleotide binding250 – 2556NAD By similarity

Sites

Active site2721 By similarity
Active site3061 By similarity

Experimental info

Sequence conflict2651H → R in CAA66106. Ref.3
Sequence conflict484 – 49916DWLDG…VCVRY → PLAGRAGC in CAA67780. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P80668 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 18D7C7D1BE136464

FASTA49953,699
        10         20         30         40         50         60 
MTEPHVAVLS QVQQFLDRQH GLYIDGRPGP AQSEKRLAIF DPATGQEIAS TADANEADVD 

        70         80         90        100        110        120 
NAVMSAWRAF VSRRWAGRLP AERERILLRF ADLVEQHSEE LAQLETLEQG KSIAISRAFE 

       130        140        150        160        170        180 
VGCTLNWMRY TAGLTTKIAG KTLDLSIPLP QGARYQAWTR KEPVGVVAGI VPWNFPLMIG 

       190        200        210        220        230        240 
MWKVMPALAA GCSIVIKPSE TTPLTMLRVA ELASEAGIPD GVFNVVTGSG AVCGAALTSH 

       250        260        270        280        290        300 
PHVAKISFTG STATGKGIAR TAADHLTRVT LELGGKNPAI VLKDADPQWV IEGLMTGSFL 

       310        320        330        340        350        360 
NQGQVCAASS RIYIEAPLFD TLVSGFEQAV KSLQVGPGMS PVAQINPLVS RAHCDKVCSF 

       370        380        390        400        410        420 
LDDAQAQQAE LIRGSNGPAG EGYYVAPTLV VNPDAKLRLT REEVFGPVVN LVRVADGEEA 

       430        440        450        460        470        480 
LQLANDTEYG LTASVWTQNL SQALEYSDRL QAGTVWVNSH TLIDANLPFG GMKQSGTGRD 

       490 
FGPDWLDGWC ETKSVCVRY 

« Hide

References

« Hide 'large scale' references
[1]"2-phenylethylamine catabolism by Escherichia coli K-12: gene organization and expression."
Hanlon S.P., Hill T.K., Flavell M.A., Stringfellow J.M., Cooper R.A.
Microbiology 143:513-518(1997) [PubMed: 9043126] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-9.
Strain: K12.
[2]Stringfellow J.M.
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"Molecular characterization of PadA, a phenylacetaldehyde dehydrogenase from Escherichia coli."
Ferrandez A., Prieto M.A., Garcia J.L., Diaz E.
FEBS Lett. 406:23-27(1997) [PubMed: 9109378] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
Strain: W / ATCC 11105 / DSM 1900.
[4]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Nucleotide sequence of the gene for monoamine oxidase (maoA) from Escherichia coli."
Azakami H., Yamashita M., Roh J.-H., Suzuki H., Kumagai H., Murooka Y.
J. Ferment. Bioeng. 77:315-319(1994)
Cited for: PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99402 Genomic DNA. Translation: CAA67780.1.
X97453 Genomic DNA. Translation: CAA66106.1.
U00096 Genomic DNA. Translation: AAC74467.2.
AP009048 Genomic DNA. Translation: BAA14992.2.
D23670 Genomic DNA. No translation available.
PIRD64889.
RefSeqNP_415903.4. NC_000913.2.

3D structure databases

ProteinModelPortalP80668.
SMRP80668. Positions 19-499.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-9581N.
IntActP80668. 1 interaction.
MINTMINT-1256983.

Proteomic databases

PRIDEP80668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000000062; EBESCP00000000062; EBESCG00000000048.
EBESCT00000015569; EBESCP00000014860; EBESCG00000014629.
GeneID945933.
GenomeReviewsGene locus JW1380 in contig AP009048_GR.
Gene locus b1385 in contig U00096_GR.
KEGGecj:JW1380.
eco:b1385.
PATRIC32118056. VBIEscCol129921_1448.

Organism-specific databases

EchoBASEEB2971.
EcoGeneEG13179. feaB.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeEBGT00050000009175.
HOGENOMHBG752218.
OMASAHHRDK.
PhylomeDBP80668.
ProtClustDBCLSK950270.

Enzyme and pathway databases

BioCycEcoCyc:PHENDEHYD-MONOMER.
MetaCyc:PHENDEHYD-MONOMER.

Gene expression databases

GenevestigatorP80668.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KOK00146.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFEAB_ECOLI
AccessionPrimary (citable) accession number: P80668
Secondary accession number(s): O32557, P46884, P77637
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families