EC 1.3.1.56
Biphenyl-2,3-dihydro-2,3-diol dehydrogenase
Biphenyl-cis-diol dehydrogenase
2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase
2,3-dihydroxy-4-phenylhexa-4,6-diene dehydrogenase

Gene name

Name:

bphB

From

Pseudomonas sp. (strain KKS102)

[TaxID: 307]

Taxonomy

Bacteria; Proteobacteria.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/bbrc.1994.2008; PubMed=8048958 [NCBI, ExPASy, EBI, Israel, Japan]
Fukuda M., Yasukochi Y., Kikuchi Y., Nagata Y., Kimbara K., Horiuchi H., Takagi M., Yano K.;
"Identification of the bphA and bphB genes of Pseudomonas sp. strains KKS102 involved in degradation of biphenyl and polychlorinated biphenyls.";
Biochem. Biophys. Res. Commun. 202:850-856(1994).

Comments

CATALYTIC ACTIVITY: Cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD⁺ = biphenyl-2,3-diol + NADH.
PATHWAY: Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoic acid and benzoic acid from biphenyl: step 2/4 .
SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D17319; BAA04140.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC2441; JC2441.

3D structure databases

HSSP

P47227; 1BDB. [HSSP ENTRY / PDB]

SMR

P50206; 1-275.

ModBase

P50206.

Ontologies

GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
GO:0018509;	Molecular function: cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0019439;	Biological process: aromatic compound catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR017711; BphB_TodD.
IPR002198; DHase_sc/Rdtase_SDR.
IPR002347; Glc/ribitol_DHase.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR19410; ADH_short_C2; 1.

Pfam

PF00106; adh_short; 1.
Pfam graphical view of domain structure.

PRINTS

PR00081; GDHRDH.
PR00080; SDRFAMILY.

PROSITE

PS00061; ADH_SHORT; 1.

Other

ProtoNet

P50206.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 276`	`276`	`Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase.`	`PRO_0000054534`
`NP_BIND`	`9 33`	`25`	`NAD (By similarity).`
`ACT_SITE`	`155 155`		`Proton acceptor (By similarity).`
`BINDING`	`142 142`		`Substrate (By similarity).`

Sequence information

Length: 276 AA [This is the length of the unprocessed precursor]

Molecular weight: 28933 Da [This is the MW of the unprocessed precursor]

CRC64: 3C000F5EA72F44D1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQLNNEVALV TGGGSGLGRA IVDRFVAEGA RVAVLDKSAA RLQELQAAHG AKVLGIEGDV 

        70         80         90        100        110        120 
RVLADHQKAA RECVAAFGKI DCLIPNAGIW DYSMPLVDIP DDRIDAAFDE VFHINVKGYL 

       130        140        150        160        170        180 
LAVKACLPAL VQSRGSVVFT ISNAGFYPNG GGPLYTGAKH AVVGMVRELA YELAPHVRVN 

       190        200        210        220        230        240 
GVAPGGMSTD LRGPASLGMA NQAISSVPLG EMLTSVLPVG RMPVRAEYTG AYVFFATRGD 

       250        260        270 
TFPTTGALLN HDGGMGVRGF FEATGGKDLP QKLRLS

P50206 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools