P39849 (XYLB_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aryl-alcohol dehydrogenase
EC=1.1.1.90

Alternative name(s):
Benzyl alcohol dehydrogenase
Short name=BADH

Gene names

Name:

xylB

Encoded on

Plasmid TOL pWW0 Ref.1
Plasmid TOL pWW53 Ref.2

Organism

Pseudomonas putida (Arthrobacter siderocapsulatus)

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Oxidizes primary alcohols with an aromatic or cyclohex-1-ene ring. It is highly specific for benzyl alcohol.
Catalytic activity	An aromatic alcohol + NAD+ = an aromatic aldehyde + NADH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.
Sequence caution	The sequence AAA26024.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	Metal-binding NAD Zinc
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing Plasmid
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aryl-alcohol dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 366	366	Aryl-alcohol dehydrogenase		PRO_0000160827
Sites
	Metal binding	40	1	Zinc 1; catalytic By similarity
	Metal binding	61	1	Zinc 1; catalytic By similarity
	Metal binding	90	1	Zinc 2 By similarity
	Metal binding	93	1	Zinc 2 By similarity
	Metal binding	96	1	Zinc 2 By similarity
	Metal binding	104	1	Zinc 2 By similarity
	Metal binding	169	1	Zinc 1; catalytic By similarity
Experimental info
	Sequence conflict	40 – 41	2	CH → PG AA sequence Ref.2
	Sequence conflict	50	1	H → G AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P39849 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 23A5203C0F96D91B	FASTA	366	38,510
	10 20 30 40 50 60 MEIKAAIVRQ KNGPFLLEHV ALNEPAEDQV LVRLVATGLC HTDLVCRDQH YPVPLPMVFG 70 80 90 100 110 120 HEGAGVVERV GSAVKKVQPG DHVVLTFYTC GSCDACLSGD PTSCANSFGP NFMGRSVTGE 130 140 150 160 170 180 CTIHDHQGAE VGASFFGQSS FATYALSYER NTVKVTKDVP LELLGPLGCG IQTGAGSVLN 190 200 210 220 230 240 ALNPPAGSAI AIFGAGAVGL SAVMAAVVAG CTTIIAVDVK ENRLELASEL GATHIINPAA 250 260 270 280 290 300 NDPIEAIKEI FADGVPYVLE TSGLPAVLTQ AILSSAIGGE IGIVGAPPMG ATVPVDINFL 310 320 330 340 350 360 LFNRKLRGIV EGQSISDIFI PRLVELYRQG KFPFDKLIKF YPFDEINRAA EDSEKGVTLK PVLRIG

References

[1]	"Kinetic studies on benzyl alcohol dehydrogenase encoded by TOL plasmid pWWO. A member of the zinc-containing long chain alcohol dehydrogenase family." Shaw J.P., Rekik M., Schwager F., Harayama S. J. Biol. Chem. 268:10842-10850(1993) [PubMed: 8496150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-8.
[2]	"Comparison of benzyl alcohol dehydrogenases and benzaldehyde dehydrogenases from the benzyl alcohol and mandelate pathways in Acinetobacter calcoaceticus and from the TOL-plasmid-encoded toluene pathway in Pseudomonas putida. N-terminal amino acid sequences, amino acid compositions and immunological cross-reactions." Chalmers R.M., Keen J.N., Fewson C.A. Biochem. J. 273:99-107(1991) [PubMed: 1989592] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-53.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D63341 Genomic DNA. Translation: BAA09664.1. M94184 Genomic DNA. Translation: AAA26024.1. Different initiation.
PIR	A46704.
RefSeq	NP_542885.1. NC_003350.1.
3D structure databases
ProteinModelPortal	P39849.
SMR	P39849. Positions 2-365.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1218744.
Phylogenomic databases
ProtClustDB	CLSK518357.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-2967.
BRENDA	1.1.1.90. 5163.
Family and domain databases
InterPro	IPR013149. ADH_C. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn-type. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
SUPFAM	SSF50129. GroES_like. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

XYLB_PSEPU

Accession

Primary (citable) accession number: P39849

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program