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Protein

Benzene 1,2-dioxygenase subunit beta

Gene

bnzB

Organism
Pseudomonas putida (strain F1 / ATCC 700007)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes both the oxidation of benzene and toluene. The beta subunit may be responsible for the substrate specificity of the enzyme.

Catalytic activityi

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+.

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster per subunit.By similarity
  • Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity

Pathwayi: benzene degradation

This protein is involved in step 1 of the subpathway that synthesizes catechol from benzene.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Benzene 1,2-dioxygenase subunit beta (bnzB), Benzene 1,2-dioxygenase subunit alpha (bnzA)
  2. no protein annotated in this organism
This subpathway is part of the pathway benzene degradation, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes catechol from benzene, the pathway benzene degradation and in Aromatic compound metabolism.

Pathwayi: toluene degradation

This protein is involved in the pathway toluene degradation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway toluene degradation and in Xenobiotic degradation.

Pathwayi: xylene degradation

This protein is involved in the pathway xylene degradation, which is part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the pathway xylene degradation and in Xenobiotic degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciPPUT351746:GI26-2928-MONOMER.
UniPathwayiUPA00228.
UPA00272; UER00391.
UPA00273.

Names & Taxonomyi

Protein namesi
Recommended name:
Benzene 1,2-dioxygenase subunit beta (EC:1.14.12.3)
Alternative name(s):
Benzene 1,2-dioxygenase P2 subunit
Toluene 2,3-dioxygenase subunit beta (EC:1.14.12.11)
Gene namesi
Name:bnzB
Synonyms:todC2
Ordered Locus Names:Pput_2880
OrganismiPseudomonas putida (strain F1 / ATCC 700007)
Taxonomic identifieri351746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000006553 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 187187Benzene 1,2-dioxygenase subunit betaPRO_0000314466Add
BLAST

Interactioni

Subunit structurei

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).

Protein-protein interaction databases

STRINGi351746.Pput_2880.

Structurei

Secondary structure

1
187
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 123Combined sources
Helixi20 – 3819Combined sources
Helixi42 – 476Combined sources
Beta strandi49 – 5810Combined sources
Helixi65 – 706Combined sources
Beta strandi79 – 835Combined sources
Helixi85 – 9410Combined sources
Helixi101 – 1033Combined sources
Beta strandi108 – 12013Combined sources
Beta strandi126 – 13914Combined sources
Turni140 – 1423Combined sources
Beta strandi143 – 15715Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi164 – 17411Combined sources
Beta strandi176 – 1816Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EN1X-ray3.20B1-187[»]
3EQQX-ray3.20B1-187[»]
ProteinModelPortaliA5W4F1.
SMRiA5W4F1. Positions 11-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA5W4F1.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108SBK. Bacteria.
COG5517. LUCA.
HOGENOMiHOG000106036.
KOiK16268.
OMAiRTTRIMR.
OrthoDBiEOG6M9DWF.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR032710. NTF2-like_dom.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamiPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.

Sequencei

Sequence statusi: Complete.

A5W4F1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIDSANRADV FLRKPAPVAP ELQHEVEQFY YWEAKLLNDR RFEEWFALLA
60 70 80 90 100
EDIHYFMPIR TTRIMRDSRL EYSGSREYAH FDDDATMMKG RLRKITSDVS
110 120 130 140 150
WSENPASRTR HLVSNVMIVG AEAEGEYEIS SAFIVYRNRL ERQLDIFAGE
160 170 180
RRDTLRRNTS EAGFEIVNRT ILIDQSTILA NNLSFFF
Length:187
Mass (Da):22,013
Last modified:July 10, 2007 - v1
Checksum:i39A5D2BECB6116B5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04996 Genomic DNA. Translation: AAA26006.1.
CP000712 Genomic DNA. Translation: ABQ79011.1.
PIRiB29830.
RefSeqiWP_012052600.1. NC_009512.1.

Genome annotation databases

EnsemblBacteriaiABQ79011; ABQ79011; Pput_2880.
KEGGippf:Pput_2880.
PATRICi19921903. VBIPsePut56420_2936.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04996 Genomic DNA. Translation: AAA26006.1.
CP000712 Genomic DNA. Translation: ABQ79011.1.
PIRiB29830.
RefSeqiWP_012052600.1. NC_009512.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EN1X-ray3.20B1-187[»]
3EQQX-ray3.20B1-187[»]
ProteinModelPortaliA5W4F1.
SMRiA5W4F1. Positions 11-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351746.Pput_2880.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ79011; ABQ79011; Pput_2880.
KEGGippf:Pput_2880.
PATRICi19921903. VBIPsePut56420_2936.

Phylogenomic databases

eggNOGiENOG4108SBK. Bacteria.
COG5517. LUCA.
HOGENOMiHOG000106036.
KOiK16268.
OMAiRTTRIMR.
OrthoDBiEOG6M9DWF.

Enzyme and pathway databases

UniPathwayiUPA00228.
UPA00272; UER00391.
UPA00273.
BioCyciPPUT351746:GI26-2928-MONOMER.

Miscellaneous databases

EvolutionaryTraceiA5W4F1.

Family and domain databases

Gene3Di3.10.450.50. 1 hit.
InterProiIPR032710. NTF2-like_dom.
IPR000391. Rng_hydr_dOase-bsu.
[Graphical view]
PfamiPF00866. Ring_hydroxyl_B. 1 hit.
[Graphical view]
SUPFAMiSSF54427. SSF54427. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: F1 / ATCC 700007.

Entry informationi

Entry nameiBNZB_PSEP1
AccessioniPrimary (citable) accession number: A5W4F1
Secondary accession number(s): P08085, P13451
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: January 20, 2016
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.