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A5W4F2 (BNZA_PSEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Ordered Locus Names:Pput_2881
OrganismPseudomonas putida (strain F1 / ATCC 700007) [Complete proteome] [HAMAP]
Taxonomic identifier351746 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 450450Benzene 1,2-dioxygenase subunit alpha
PRO_0000314465

Regions

Domain54 – 163110Rieske

Sites

Metal binding961Iron-sulfur (2Fe-2S) By similarity
Metal binding981Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Metal binding1161Iron-sulfur (2Fe-2S) By similarity
Metal binding1191Iron-sulfur (2Fe-2S); via pros nitrogen By similarity
Metal binding2221Iron By similarity
Metal binding2281Iron By similarity

Secondary structure

.............................................................................................. 450
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
A5W4F2 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 038C80F197F3485D

FASTA45050,944
        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 

« Hide

References

« Hide 'large scale' references
[1]"Toluene degradation by Pseudomonas putida F1. Nucleotide sequence of the todC1C2BADE genes and their expression in Escherichia coli."
Zylstra G.J., Gibson D.T.
J. Biol. Chem. 264:14940-14946(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12.
[2]"Complete sequence of Pseudomonas putida F1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F1 / ATCC 700007.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04996 Genomic DNA. Translation: AAA26005.1.
CP000712 Genomic DNA. Translation: ABQ79012.1.
PIRA36516.
RefSeqYP_001268196.1. NC_009512.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3EN1X-ray3.20A1-450[»]
3EQQX-ray3.20A1-450[»]
ProteinModelPortalA5W4F2.
SMRA5W4F2. Positions 15-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351746.Pput_2881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ79012; ABQ79012; Pput_2881.
GeneID5195399.
KEGGppf:Pput_2881.
PATRIC19921905. VBIPsePut56420_2937.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4638.
HOGENOMHOG000105925.
KOK03268.
OMAYWTEGPA.
OrthoDBEOG6W19DT.
ProtClustDBCLSK880425.

Enzyme and pathway databases

BioCycPPUT351746:GI26-2929-MONOMER.
UniPathwayUPA00228.
UPA00272; UER00391.
UPA00273.

Family and domain databases

Gene3D2.102.10.10. 1 hit.
3.90.380.10. 1 hit.
InterProIPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879. Ring_hydroxy_dOase_asu_C_dom.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
PfamPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSPR00090. RNGDIOXGNASE.
SUPFAMSSF50022. SSF50022. 1 hit.
PROSITEPS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceA5W4F2.

Entry information

Entry nameBNZA_PSEP1
AccessionPrimary (citable) accession number: A5W4F2
Secondary accession number(s): P08084, P13450
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: November 13, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways