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Protein

Benzene 1,2-dioxygenase subunit alpha

Gene

bnzA

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.

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)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

BioCyciPPUT351746:GI26-2929-MONOMER.
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 F1 / ATCC 700007)
Taxonomic identifieri351746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000006553 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 450450Benzene 1,2-dioxygenase subunit alphaPRO_0000314465Add
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

Secondary structure

1
450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi17 – 226Combined sources
Turni26 – 294Combined sources
Helixi33 – 364Combined sources
Helixi39 – 4810Combined sources
Helixi50 – 523Combined sources
Beta strandi55 – 595Combined sources
Helixi60 – 623Combined sources
Beta strandi68 – 747Combined sources
Beta strandi77 – 837Combined sources
Beta strandi89 – 957Combined sources
Turni97 – 993Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi112 – 1154Combined sources
Turni117 – 1193Combined sources
Beta strandi122 – 1243Combined sources
Beta strandi129 – 1313Combined sources
Helixi135 – 1384Combined sources
Turni144 – 1474Combined sources
Beta strandi153 – 1575Combined sources
Beta strandi160 – 1645Combined sources
Helixi172 – 1765Combined sources
Helixi177 – 1793Combined sources
Helixi180 – 1878Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi194 – 20512Combined sources
Helixi209 – 21810Combined sources
Helixi220 – 2234Combined sources
Turni224 – 2285Combined sources
Helixi229 – 2346Combined sources
Beta strandi251 – 2555Combined sources
Beta strandi257 – 2604Combined sources
Beta strandi262 – 2687Combined sources
Helixi271 – 28616Combined sources
Helixi289 – 29810Combined sources
Helixi301 – 3055Combined sources
Beta strandi311 – 3144Combined sources
Turni315 – 3173Combined sources
Beta strandi318 – 3203Combined sources
Turni322 – 3243Combined sources
Beta strandi326 – 3327Combined sources
Beta strandi334 – 3363Combined sources
Beta strandi338 – 34710Combined sources
Helixi352 – 36514Combined sources
Beta strandi366 – 3694Combined sources
Helixi373 – 38614Combined sources
Helixi391 – 3933Combined sources
Turni401 – 4044Combined sources
Beta strandi406 – 4083Combined sources
Beta strandi411 – 4133Combined sources
Beta strandi415 – 4195Combined sources
Helixi425 – 43814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3EN1X-ray3.20A1-450[»]
3EQQX-ray3.20A1-450[»]
ProteinModelPortaliA5W4F2.
SMRiA5W4F2. Positions 15-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA5W4F2.

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.
HOGENOMiHOG000105925.
KOiK03268.
OMAiFREPKAQ.
OrthoDBiEOG6W19DT.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
3EN1X-ray3.20A1-450[»]
3EQQX-ray3.20A1-450[»]
ProteinModelPortaliA5W4F2.
SMRiA5W4F2. Positions 15-450.
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.
OrthoDBiEOG6W19DT.

Enzyme and pathway databases

UniPathwayiUPA00228.
UPA00272; UER00391.
UPA00273.
BioCyciPPUT351746:GI26-2929-MONOMER.

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...

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 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 11, 2015
This is version 62 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.