Reviewed, UniProtKB/Swiss-Prot P0C618 (BNZA_PSEPU)

Names and origin

Protein names

Recommended name:
    Benzene 1,2-dioxygenase subunit alpha
    EC=1.14.12.3
Alternative name(s):
    Benzene 1,2-dioxygenase P1 subunit
    Toluene 2,3-dioxygenase subunit alpha
    EC=1.14.12.11

Gene names

Name:	bnzA
Synonyms:	todC1

Organism

Pseudomonas putida

Taxonomic identifier

303 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes both the oxidation of benzene and toluene.
Catalytic activity	Benzene + NADH + O2 = cis-cyclohexa-3,5-diene-1,2-diol + NAD+. Toluene + NADH + O2 = (1S,2R)-3-methylcyclohexa-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	Aromatic compound metabolism; benzene degradation; catechol from benzene: step 1/2. Xenobiotic degradation; toluene degradation. Xenobiotic degradation; xylene degradation.
Subunit structure	This dioxygenase system consists of four proteins: the two subunits of the hydroxylase component (bnzA and bnzB), a ferredoxin (bnzC) and a ferredoxin reductase (bnzD).
Sequence similarities	Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. Contains 1 Rieske domain.
Sequence caution	The sequence AAA25735.1 differs from that shown. Reason: Frameshift at positions 330, 339, 360, 362, 368 and 393.

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 benzene 1,2-dioxygenase activity Inferred from electronic annotation. Source: EC 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 toluene dioxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 450	450	Benzene 1,2-dioxygenase subunit alpha		PRO_0000085045
Regions
	Domain	54 – 163	110	Rieske
Sites
	Metal binding	96	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	98	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	116	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	119	1	Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
	Metal binding	222	1	Iron By similarity
	Metal binding	228	1	Iron By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0C618-1 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: 038C80F197F3485D	FASTA	450	50,944
	10 20 30 40 50 60 MNQTDTSPIR LRRSWNTSEI EALFDEHAGR IDPRIYTDED LYQLELERVF ARSWLLLGHE 70 80 90 100 110 120 TQIRKPGDYI TTYMGEDPVV VVRQKDASIA VFLNQCRHRG MRICRADAGN AKAFTCSYHG 130 140 150 160 170 180 WAYDTAGNLV NVPYEAESFA CLNKKEWSPL KARVETYKGL IFANWDENAV DLDTYLGEAK 190 200 210 220 230 240 FYMDHMLDRT EAGTEAIPGV QKWVIPCNWK FAAEQFCSDM YHAGTTSHLS GILAGLPEDL 250 260 270 280 290 300 EMADLAPPTV GKQYRASWGG HGSGFYVGDP NLMLAIMGPK VTSYWTEGPA SEKAAERLGS 310 320 330 340 350 360 VERGSKLMVE HMTVFPTCSF LPGINTVRTW HPRGPNEVEV WAFTVVDADA PDDIKEEFRR 370 380 390 400 410 420 QTLRTFSAGG VFEQDDGENW VEIQHILRGH KARSRPFNAE MSMDQTVDND PVYPGRISNN 430 440 450 VYSEEAARGL YAHWLRMMTS PDWDALKATR

References

[1]	"Nucleotide sequencing and characterization of the genes encoding benzene oxidation enzymes of Pseudomonas putida." Irie S., Doi S., Yorifuji T., Takagi M., Yano K. J. Bacteriol. 169:5174-5179(1987) [PubMed: 3667527] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BE-81.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M17904 Genomic DNA. Translation: AAA25735.1. Frameshift.
PIR	A29830.
3D structure databases
SMR	P0C618. Positions 15-450.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.12.11. 403. 1.14.12.3. 403.
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]
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

BNZA_PSEPU

Accession

Primary (citable) accession number: P0C618
Secondary accession number(s): P08084, P13450

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	January 19, 2010
This is version 12 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)