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Protein

Benzene 1,2-dioxygenase subunit alpha

Gene

bnzA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

Functioni

Catalyzes both the oxidation of benzene and toluene.

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] clusterPROSITE-ProRule annotationNote: Binds 1 [2Fe-2S] cluster per subunit.PROSITE-ProRule annotation
  • 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 system ferredoxin subunit (bedB), Benzene 1,2-dioxygenase subunit beta (bedC2), Benzene 1,2-dioxygenase system ferredoxin subunit (bnzC), Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit (bedA), Benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component (bnzD), Benzene 1,2-dioxygenase subunit alpha (bedC1), Benzene 1,2-dioxygenase subunit beta (bnzB), Benzene 1,2-dioxygenase subunit alpha (bnzA)
  2. Cis-1,2-dihydrobenzene-1,2-diol dehydrogenase (bnzE)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi96 – 961Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi98 – 981Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotation
Metal bindingi116 – 1161Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi119 – 1191Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotation
Metal bindingi222 – 2221IronBy similarity
Metal bindingi228 – 2281IronBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

2Fe-2S, Iron, Iron-sulfur, Metal-binding, NAD

Enzyme and pathway databases

UniPathwayiUPA00228.
UPA00272; UER00391.
UPA00273.

Names & Taxonomyi

Protein namesi
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 namesi
Name:bnzA
Synonyms:todC1
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Benzene 1,2-dioxygenase subunit alphaPRO_0000085045Add
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_2881.

Structurei

3D structure databases

ProteinModelPortaliP0C618.
SMRiP0C618. Positions 15-450.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 163110RieskePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Rieske domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105FUY. Bacteria.
COG4638. LUCA.

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
3.90.380.10. 1 hit.
InterProiIPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879. Ring_hydroxy_dOase_asu_C_dom.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
PfamiPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSiPR00090. RNGDIOXGNASE.
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C618-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQTDTSPIR LRRSWNTSEI EALFDEHAGR IDPRIYTDED LYQLELERVF
60 70 80 90 100
ARSWLLLGHE TQIRKPGDYI TTYMGEDPVV VVRQKDASIA VFLNQCRHRG
110 120 130 140 150
MRICRADAGN AKAFTCSYHG WAYDTAGNLV NVPYEAESFA CLNKKEWSPL
160 170 180 190 200
KARVETYKGL IFANWDENAV DLDTYLGEAK FYMDHMLDRT EAGTEAIPGV
210 220 230 240 250
QKWVIPCNWK FAAEQFCSDM YHAGTTSHLS GILAGLPEDL EMADLAPPTV
260 270 280 290 300
GKQYRASWGG HGSGFYVGDP NLMLAIMGPK VTSYWTEGPA SEKAAERLGS
310 320 330 340 350
VERGSKLMVE HMTVFPTCSF LPGINTVRTW HPRGPNEVEV WAFTVVDADA
360 370 380 390 400
PDDIKEEFRR QTLRTFSAGG VFEQDDGENW VEIQHILRGH KARSRPFNAE
410 420 430 440 450
MSMDQTVDND PVYPGRISNN VYSEEAARGL YAHWLRMMTS PDWDALKATR
Length:450
Mass (Da):50,944
Last modified:January 15, 2008 - v1
Checksum:i038C80F197F3485D
GO

Sequence cautioni

The sequence AAA25735 differs from that shown. Reason: Frameshift at positions 330, 339, 360, 362, 368 and 393. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17904 Genomic DNA. Translation: AAA25735.1. Frameshift.
PIRiA29830.
RefSeqiWP_012052601.1. NZ_BBNC01000005.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17904 Genomic DNA. Translation: AAA25735.1. Frameshift.
PIRiA29830.
RefSeqiWP_012052601.1. NZ_BBNC01000005.1.

3D structure databases

ProteinModelPortaliP0C618.
SMRiP0C618. Positions 15-450.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351746.Pput_2881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105FUY. Bacteria.
COG4638. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00228.
UPA00272; UER00391.
UPA00273.

Family and domain databases

Gene3Di2.102.10.10. 1 hit.
3.90.380.10. 1 hit.
InterProiIPR017941. Rieske_2Fe-2S.
IPR015881. Ring-hydroxy_dOase_2Fe2S_BS.
IPR015879. Ring_hydroxy_dOase_asu_C_dom.
IPR001663. Rng_hydr_dOase-A.
[Graphical view]
PfamiPF00355. Rieske. 1 hit.
PF00848. Ring_hydroxyl_A. 1 hit.
[Graphical view]
PRINTSiPR00090. RNGDIOXGNASE.
SUPFAMiSSF50022. SSF50022. 1 hit.
PROSITEiPS51296. RIESKE. 1 hit.
PS00570. RING_HYDROXYL_ALPHA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBNZA_PSEPU
AccessioniPrimary (citable) accession number: P0C618
Secondary accession number(s): P08084, P13450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: November 11, 2015
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.