Q46372 (BPHA_COMTE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Biphenyl dioxygenase subunit alpha
EC=1.14.12.18

Alternative name(s):
Biphenyl 2,3-dioxygenase

Gene names

Name:

bphA

Organism

Comamonas testosteroni (Pseudomonas testosteroni)

Taxonomic identifier

285 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Biphenyl + NADH + O2 = (1S,2R)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+.
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity. Binds 1 iron ion per subunit By similarity.
Pathway	Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl: step 1/4.
Subunit structure	Heterohexamer consisting of three BphA subunits and three BphE subunits. A ferredoxin (BphF) and a ferredoxin reductase (BphG) must be present to obtain activity By similarity.
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. Contains 1 Rieske domain.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding NAD
Molecular function	Dioxygenase Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW biphenyl 2,3-dioxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 457

457

Biphenyl dioxygenase subunit alpha

PRO_0000085047

Regions

Domain

58 – 174

117

Rieske

Sites

Metal binding

100

1

Iron-sulfur (2Fe-2S) By similarity

Metal binding

102

1

Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Metal binding

120

1

Iron-sulfur (2Fe-2S) By similarity

Metal binding

123

1

Iron-sulfur (2Fe-2S); via pros nitrogen By similarity

Metal binding

233

1

Iron By similarity

Metal binding

239

1

Iron By similarity

Secondary structure

1

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457

Helix Strand Turn

Details...

Helix

21 – 25

5

Helix

37 – 40

4

Helix

43 – 52

10

Helix

64 – 66

3

Beta strand

73 – 77

5

Beta strand

82 – 87

6

Beta strand

93 – 98

6

Beta strand

116 – 119

4

Beta strand

126 – 128

3

Beta strand

133 – 135

3

Helix

139 – 143

5

Helix

155 – 157

3

Beta strand

162 – 167

6

Beta strand

172 – 176

5

Helix

183 – 186

4

Turn

187 – 189

3

Helix

191 – 198

8

Beta strand

199 – 201

3

Beta strand

212 – 218

7

Helix

220 – 229

10

Turn

253 – 255

3

Beta strand

277 – 279

3

Helix

282 – 287

6

Helix

291 – 297

7

Helix

301 – 308

8

Helix

314 – 316

3

Beta strand

322 – 324

3

Turn

325 – 327

3

Beta strand

328 – 331

4

Beta strand

336 – 343

8

Beta strand

348 – 356

9

Helix

362 – 375

14

Turn

383 – 385

3

Helix

389 – 396

8

Helix

402 – 404

3

Turn

434 – 436

3

Helix

440 – 448

9

Helix

452 – 455

4

Sequences

	Sequence		Length	Mass (Da)
	Q46372 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D133FC0635FACBF5	FASTA	457	51,692
	10 20 30 40 50 60 MSSTMKDTQE APVRWSRNWT PDAIRALVDQ DNGKLDARIY ADQDLYQLEL ERVFGRSWLM 70 80 90 100 110 120 LGHETHIPKI GDYLTTYMGE DPVIMVRQKD QSIKVFLNQC RHRGMRIVRS DGGNAKAFTC 130 140 150 160 170 180 TYHGWAYDIA GNLVNVPFEK EAFCDKKEGD CGFDKADWGP LQARVETYKG LVFANWDPEA 190 200 210 220 230 240 PDLKTYLSDA MPYMDVMLDR TEAGTEAIGG IQKWVIPCNW KFAAEQFCSD MYHAGTMSHL 250 260 270 280 290 300 SGVLAGLPPE MDLTQIQLSK NGNQFRSAWG GHGAGWFIND SSILLSVVGP KITQYWTQGP 310 320 330 340 350 360 AAEKAARRVP QLPILDMFGQ HMTVFPTCSF LPGINTIRTW HPRGPNEVEV WAFVLVDADA 370 380 390 400 410 420 PEDIKEEFRL QNIRTFNAGG VFEQDDGENW VEIQRVMRGH KAKSTSLCAK MGLNVPNKNN 430 440 450 PAYPGKTAYV YAEEAARGMY HHWSRMMSEP SWDTLKP

References

[1]

"Sequencing of Comamonas testosteroni strain B-356-biphenyl/chlorobiphenyl dioxygenase genes: evolutionary relationships among Gram-negative bacterial biphenyl dioxygenases." Sylvestre M., Sirois M., Hurtubise Y., Bergeron J., Ahmad D., Shareck F., Barriault D., Guillemette I., Juteau J.-M. Gene 174:195-202(1996) [PubMed: 8890734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B-356.

+

Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U47637 Genomic DNA. Translation: AAC44526.1.

PIR

JC4993.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GZX	X-ray	1.58	A	1-457	[»]
3GZY	X-ray	1.62	A	1-457	[»]

ProteinModelPortal

Q46372.

SMR

Q46372. Positions 18-456.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

1.14.12.18. 1590.

Family and domain databases

InterPro

IPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879. Ring_hydroxy_dOase_asu_C.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]

Gene3D

G3DSA:2.102.10.10. Rieske_reg. 1 hit.

Pfam

PF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]

PRINTS

PR00090. RNGDIOXGNASE.

SUPFAM

SSF50022. Rieske_dom. 1 hit.

PROSITE

PS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

BPHA_COMTE

Accession

Primary (citable) accession number: Q46372

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	June 28, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program