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Protein

Phenylacetaldehyde dehydrogenase

Gene

feaB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Phenylacetaldehyde + NAD+ + H2O = phenylacetate + NADH.

Pathwayi: L-phenylalanine degradation

This protein is involved in step 3 of the subpathway that synthesizes phenylacetate from L-phenylalanine.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Primary amine oxidase (tynA)
  3. Phenylacetaldehyde dehydrogenase (feaB)
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phenylacetate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei272By similarity1
Active sitei306By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi250 – 255NADBy similarity6

GO - Molecular functioni

  • 4-hydroxyphenylacetaldehyde dehydrogenase activity Source: EcoliWiki
  • oxidoreductase activity Source: EcoliWiki
  • phenylacetaldehyde dehydrogenase activity Source: EcoliWiki

GO - Biological processi

  • 4-nitrophenol catabolic process Source: EcoliWiki
  • L-phenylalanine catabolic process Source: UniProtKB-UniPathway
  • NAD biosynthetic process Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciEcoCyc:PHENDEHYD-MONOMER.
ECOL316407:JW1380-MONOMER.
MetaCyc:PHENDEHYD-MONOMER.
BRENDAi1.2.1.39. 2026.
UniPathwayiUPA00139; UER00724.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylacetaldehyde dehydrogenase (EC:1.2.1.39)
Short name:
PAD
Gene namesi
Name:feaB
Synonyms:maoB, padA, ydbG
Ordered Locus Names:b1385, JW1380
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13179. feaB.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000565751 – 499Phenylacetaldehyde dehydrogenaseAdd BLAST499

Proteomic databases

EPDiP80668.
PaxDbiP80668.
PRIDEiP80668.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi4261813. 11 interactors.
DIPiDIP-9581N.
IntActiP80668. 1 interactor.
MINTiMINT-1256983.
STRINGi511145.b1385.

Structurei

3D structure databases

ProteinModelPortaliP80668.
SMRiP80668.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
InParanoidiP80668.
KOiK00146.
OMAiINISRAF.
PhylomeDBiP80668.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P80668-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEPHVAVLS QVQQFLDRQH GLYIDGRPGP AQSEKRLAIF DPATGQEIAS
60 70 80 90 100
TADANEADVD NAVMSAWRAF VSRRWAGRLP AERERILLRF ADLVEQHSEE
110 120 130 140 150
LAQLETLEQG KSIAISRAFE VGCTLNWMRY TAGLTTKIAG KTLDLSIPLP
160 170 180 190 200
QGARYQAWTR KEPVGVVAGI VPWNFPLMIG MWKVMPALAA GCSIVIKPSE
210 220 230 240 250
TTPLTMLRVA ELASEAGIPD GVFNVVTGSG AVCGAALTSH PHVAKISFTG
260 270 280 290 300
STATGKGIAR TAADHLTRVT LELGGKNPAI VLKDADPQWV IEGLMTGSFL
310 320 330 340 350
NQGQVCAASS RIYIEAPLFD TLVSGFEQAV KSLQVGPGMS PVAQINPLVS
360 370 380 390 400
RAHCDKVCSF LDDAQAQQAE LIRGSNGPAG EGYYVAPTLV VNPDAKLRLT
410 420 430 440 450
REEVFGPVVN LVRVADGEEA LQLANDTEYG LTASVWTQNL SQALEYSDRL
460 470 480 490
QAGTVWVNSH TLIDANLPFG GMKQSGTGRD FGPDWLDGWC ETKSVCVRY
Length:499
Mass (Da):53,699
Last modified:November 1, 1997 - v2
Checksum:i18D7C7D1BE136464
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti265H → R in CAA66106 (PubMed:9109378).Curated1
Sequence conflicti484 – 499DWLDG…VCVRY → PLAGRAGC in CAA67780 (PubMed:9043126).CuratedAdd BLAST16

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD64889.
RefSeqiNP_415903.4. NC_000913.3.
WP_000138615.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74467; AAC74467; b1385.
BAA14992; BAA14992; BAA14992.
GeneIDi945933.
KEGGiecj:JW1380.
eco:b1385.
PATRICi32118056. VBIEscCol129921_1448.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiD64889.
RefSeqiNP_415903.4. NC_000913.3.
WP_000138615.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP80668.
SMRiP80668.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261813. 11 interactors.
DIPiDIP-9581N.
IntActiP80668. 1 interactor.
MINTiMINT-1256983.
STRINGi511145.b1385.

Proteomic databases

EPDiP80668.
PaxDbiP80668.
PRIDEiP80668.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74467; AAC74467; b1385.
BAA14992; BAA14992; BAA14992.
GeneIDi945933.
KEGGiecj:JW1380.
eco:b1385.
PATRICi32118056. VBIEscCol129921_1448.

Organism-specific databases

EchoBASEiEB2971.
EcoGeneiEG13179. feaB.

Phylogenomic databases

eggNOGiENOG4105C26. Bacteria.
COG1012. LUCA.
HOGENOMiHOG000271505.
InParanoidiP80668.
KOiK00146.
OMAiINISRAF.
PhylomeDBiP80668.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00724.
BioCyciEcoCyc:PHENDEHYD-MONOMER.
ECOL316407:JW1380-MONOMER.
MetaCyc:PHENDEHYD-MONOMER.
BRENDAi1.2.1.39. 2026.

Miscellaneous databases

PROiP80668.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFEAB_ECOLI
AccessioniPrimary (citable) accession number: P80668
Secondary accession number(s): O32557, P46884, P77637
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Can also use NADP, but prefers NAD.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.