Reviewed, UniProtKB/Swiss-Prot Q46372 (BPHA_COMTE)

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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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-pentadienoic acid and benzoic acid 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
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction 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 electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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

Sequences

	Sequence		Length	Mass (Da)
	Q46372-1 [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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U47637 Genomic DNA. Translation: AAC44526.1.
PIR	JC4993.
3D structure databases
HSSP	HSSP built from PDB template 1O7N based on UniProtKB P23094.
SMR	Q46372. Positions 18-456.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.12.18. 4566.
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.
PANTHER	PTHR21266:SF2. Rng_hydr_dOase-A. 1 hit.
Pfam	PF00355. Rieske. 1 hit. PF00848. Ring_hydroxyl_A. 1 hit. [Graphical view]
PRINTS	PR00090. RNGDIOXGNASE.
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 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)