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 pseudoalcaligenes

[TaxID: 330]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas.

Protein existence

3: Inferred from homology;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=KF707; PubMed=3793719 [NCBI, ExPASy, EBI, Israel, Japan] Furukawa K., Arimura N., Miyazaki T.; "Nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene of Pseudomonas pseudoalcaligenes."; J. Bacteriol. 169:427-429(1987).

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

M15333; AAA25752.1; ALT_INIT; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P47227; 1BDB. [HSSP ENTRY / PDB]

SMR

P08694; 1-274.

ModBase

P08694.

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

P08694.

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`	`1 275`	`275`	`Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase.`	`PRO_0000054533`
`NP_BIND`	`9 33`	`25`	`NAD (By similarity).`
`ACT_SITE`	`153 153`		`Proton acceptor (By similarity).`
`BINDING`	`140 140`		`Substrate (By similarity).`

Sequence information

Length: 275 AA [This is the length of the unprocessed precursor]

Molecular weight: 28726 Da [This is the MW of the unprocessed precursor]

CRC64: F32A4A870B47E566 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLKGEAVLI TGGASGLGRA LVDRFVAEAK VAVLDKSAER LAELETDLGD NVLGIVGDVR 

        70         80         90        100        110        120 
SLEDQKQAAS RCVARFGKID TLIPNAGIWD YSTALVDLPE ESLDAAFDEV FHINVKGYIH 

       130        140        150        160        170        180 
AVKALPALVA SRGNVIFTIS NAGFYPNGGG PLYTAAKQAI VGLVRELAFE LAPYVRVNGV 

       190        200        210        220        230        240 
GPGGMNSDMR GPSSLGMGSK AISTVPLADM LKSVLPIGRM PEVEEYTGAY VFFATRGDAA 

       250        260        270 
PASGALVNYD GGLGVRGFFS GAGGNDLLEQ LNIHP

P08694 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