Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Benzene 1,2-dioxygenase subunit alpha

Gene

bnzA

Organism
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi96Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi98Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotation1
Metal bindingi116Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi119Iron-sulfur (2Fe-2S); via pros nitrogenPROSITE-ProRule annotation1
Metal bindingi222IronBy similarity1
Metal bindingi228IronBy similarity1

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
Ordered Locus Names:Pput_2881
OrganismiPseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Taxonomic identifieri351746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000006553 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003144651 – 450Benzene 1,2-dioxygenase subunit alphaAdd BLAST450

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

Secondary structure

1450
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi17 – 22Combined sources6
Turni26 – 29Combined sources4
Helixi33 – 36Combined sources4
Helixi39 – 48Combined sources10
Helixi50 – 52Combined sources3
Beta strandi55 – 59Combined sources5
Helixi60 – 62Combined sources3
Beta strandi68 – 74Combined sources7
Beta strandi77 – 83Combined sources7
Beta strandi89 – 95Combined sources7
Turni97 – 99Combined sources3
Beta strandi106 – 110Combined sources5
Beta strandi112 – 115Combined sources4
Turni117 – 119Combined sources3
Beta strandi122 – 124Combined sources3
Beta strandi129 – 131Combined sources3
Helixi135 – 138Combined sources4
Turni144 – 147Combined sources4
Beta strandi153 – 157Combined sources5
Beta strandi160 – 164Combined sources5
Helixi172 – 176Combined sources5
Helixi177 – 179Combined sources3
Helixi180 – 187Combined sources8
Beta strandi188 – 190Combined sources3
Beta strandi194 – 205Combined sources12
Helixi209 – 218Combined sources10
Helixi220 – 223Combined sources4
Turni224 – 228Combined sources5
Helixi229 – 234Combined sources6
Beta strandi251 – 255Combined sources5
Beta strandi257 – 260Combined sources4
Beta strandi262 – 268Combined sources7
Helixi271 – 286Combined sources16
Helixi289 – 298Combined sources10
Helixi301 – 305Combined sources5
Beta strandi311 – 314Combined sources4
Turni315 – 317Combined sources3
Beta strandi318 – 320Combined sources3
Turni322 – 324Combined sources3
Beta strandi326 – 332Combined sources7
Beta strandi334 – 336Combined sources3
Beta strandi338 – 347Combined sources10
Helixi352 – 365Combined sources14
Beta strandi366 – 369Combined sources4
Helixi373 – 386Combined sources14
Helixi391 – 393Combined sources3
Turni401 – 404Combined sources4
Beta strandi406 – 408Combined sources3
Beta strandi411 – 413Combined sources3
Beta strandi415 – 419Combined sources5
Helixi425 – 438Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EN1X-ray3.20A1-450[»]
3EQQX-ray3.20A1-450[»]
ProteinModelPortaliA5W4F2.
SMRiA5W4F2.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA5W4F2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini54 – 163RieskePROSITE-ProRule annotationAdd BLAST110

Sequence similaritiesi

Contains 1 Rieske domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105FUY. Bacteria.
COG4638. LUCA.
HOGENOMiHOG000105925.
KOiK03268.
OMAiFREPKAQ.

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.

A5W4F2-1 [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:July 10, 2007 - v1
Checksum:i038C80F197F3485D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04996 Genomic DNA. Translation: AAA26005.1.
CP000712 Genomic DNA. Translation: ABQ79012.1.
PIRiA36516.
RefSeqiWP_012052601.1. NC_009512.1.

Genome annotation databases

EnsemblBacteriaiABQ79012; ABQ79012; Pput_2881.
KEGGippf:Pput_2881.
PATRICi19921905. VBIPsePut56420_2937.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04996 Genomic DNA. Translation: AAA26005.1.
CP000712 Genomic DNA. Translation: ABQ79012.1.
PIRiA36516.
RefSeqiWP_012052601.1. NC_009512.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EN1X-ray3.20A1-450[»]
3EQQX-ray3.20A1-450[»]
ProteinModelPortaliA5W4F2.
SMRiA5W4F2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi351746.Pput_2881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABQ79012; ABQ79012; Pput_2881.
KEGGippf:Pput_2881.
PATRICi19921905. VBIPsePut56420_2937.

Phylogenomic databases

eggNOGiENOG4105FUY. Bacteria.
COG4638. LUCA.
HOGENOMiHOG000105925.
KOiK03268.
OMAiFREPKAQ.

Enzyme and pathway databases

UniPathwayiUPA00228.
UPA00272; UER00391.
UPA00273.

Miscellaneous databases

EvolutionaryTraceiA5W4F2.

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_PSEP1
AccessioniPrimary (citable) accession number: A5W4F2
Secondary accession number(s): P08084, P13450
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: November 2, 2016
This is version 65 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.