P80668 (FEAB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenylacetaldehyde dehydrogenase
Short name=PAD
EC=1.2.1.39

Gene names

Name:	feaB
Synonyms:	maoB, padA, ydbG
Ordered Locus Names:	b1385, JW1380

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	499 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	4-nitrophenol catabolic process Inferred from direct assay Ref.3. Source: EcoliWiki NAD biosynthetic process Inferred from direct assay Ref.1Ref.3. Source: EcoliWiki
Molecular function	4-hydroxyphenylacetaldehyde dehydrogenase activity Inferred from direct assay Ref.1. Source: EcoliWiki phenylacetaldehyde dehydrogenase activity Inferred from direct assay Ref.3. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 499	499	Phenylacetaldehyde dehydrogenase		PRO_0000056575
Regions
	Nucleotide binding	250 – 255	6	NAD By similarity
Sites
	Active site	272	1	By similarity
	Active site	306	1	By similarity
Experimental info
	Sequence conflict	265	1	H → R in CAA66106. Ref.3
	Sequence conflict	484 – 499	16	DWLDG…VCVRY → PLAGRAGC in CAA67780. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P80668 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 18D7C7D1BE136464	FASTA	499	53,699
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
PIR	D64889.
RefSeq	NP_415903.4. NC_000913.2.
3D structure databases
ProteinModelPortal	P80668.
SMR	P80668. Positions 19-499.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9581N.
IntAct	P80668. 1 interaction.
MINT	MINT-1256983.
Proteomic databases
PRIDE	P80668.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000000062; EBESCP00000000062; EBESCG00000000048. EBESCT00000015569; EBESCP00000014860; EBESCG00000014629.
GeneID	945933.
GenomeReviews	Gene locus JW1380 in contig AP009048_GR. Gene locus b1385 in contig U00096_GR.
KEGG	ecj:JW1380. eco:b1385.
PATRIC	32118056. VBIEscCol129921_1448.
Organism-specific databases
EchoBASE	EB2971.
EcoGene	EG13179. feaB.
Phylogenomic databases
eggNOG	COG1012.
GeneTree	EBGT00050000009175.
HOGENOM	HBG752218.
OMA	SAHHRDK.
PhylomeDB	P80668.
ProtClustDB	CLSK950270.
Enzyme and pathway databases
BioCyc	EcoCyc:PHENDEHYD-MONOMER. MetaCyc:PHENDEHYD-MONOMER.
Gene expression databases
Genevestigator	P80668.
Family and domain databases
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. [Graphical view]
Gene3D	G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KO	K00146.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FEAB_ECOLI

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program