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P21394 (XYLA_PSEPU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Xylene monooxygenase electron transfer component

Including the following 2 domains:

  1. Ferredoxin
  2. Ferredoxin--NAD(+) reductase
    EC=1.18.1.3
Gene names
Name:xylA
Encoded onPlasmid TOL pWW0
OrganismPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifier303 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidizes toluene and xylenes to (methyl)benzyl alcohols. The enzyme has a broad specificity and also oxidizes (methyl)benzyl alcohols to (methyl)benzaldehydes and indole to indoxyl.

Catalytic activity

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactor

FAD.

Binds 1 2Fe-2S cluster per subunit By similarity.

Subunit structure

Composed of two subunits: xylA and xylM.

Sequence similarities

Belongs to the bacterial ring-hydroxylating dioxygenase ferredoxin reductase family.

Contains 1 2Fe-2S ferredoxin-type domain.

Contains 1 FAD-binding FR-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350Xylene monooxygenase electron transfer component
PRO_0000167660

Regions

Domain16 – 108932Fe-2S ferredoxin-type
Domain114 – 213100FAD-binding FR-type
Region109 – 350242Ferredoxin--NADH reductase

Sites

Metal binding521Iron-sulfur (2Fe-2S) By similarity
Metal binding571Iron-sulfur (2Fe-2S) By similarity
Metal binding601Iron-sulfur (2Fe-2S) By similarity
Metal binding921Iron-sulfur (2Fe-2S) By similarity

Sequences

Sequence LengthMass (Da)Tools
P21394 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 26828AC2226C1DDD

FASTA35038,455
        10         20         30         40         50         60 
MNEFFKKISG LFVPPPESTV SVRGQGFQFK VPRGQTILES ALHQGIAFPH DCKVGSCGTC 

        70         80         90        100        110        120 
KYKLISGRVN ELTSSAMGLS GDLYQSGYRL GCQCIPKEDL EIELDTVLGQ ALVPIETSAL 

       130        140        150        160        170        180 
ISKQKRLAHD IVEMEVVPDK QIAFYPGQYA DVECAECSAV RSYSFSAPPQ PDGSLSFHVR 

       190        200        210        220        230        240 
LVPGGVFSGW LFGGDRTGAT LTLRAPYGQF GLHESNATMV CVAGGTGLAP IKCVLQSMTQ 

       250        260        270        280        290        300 
AQRERDVLLF FGARQQRDLY CLDEIEALQL DWGGRFELIP VLSEESSTSS WKGKRGMVTE 

       310        320        330        340        350 
YFKEYLTGQP YEGYLCGPPP MVDAAETELV RLGVARELVF ADRFYNRPPC 

« Hide

References

[1]"Primary structure of xylene monooxygenase: similarities to and differences from the alkane hydroxylation system."
Suzuki M., Hayakawa T., Shaw J.P., Rekik M., Harayama S.
J. Bacteriol. 173:1690-1695(1991) [PubMed: 1999388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 6-16.
[2]"Purification and characterisation of the NADH:acceptor reductase component of xylene monooxygenase encoded by the TOL plasmid pWW0 of Pseudomonas putida mt-2."
Shaw J.P., Harayama S.
Eur. J. Biochem. 209:51-61(1992) [PubMed: 1327782] [Abstract]
Cited for: CHARACTERIZATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37480 Genomic DNA. Translation: AAA26027.1.
D63341 Genomic DNA. Translation: BAA09663.1.
PIRB37316.
RefSeqNP_542886.1. NC_003350.1.

3D structure databases

ProteinModelPortalP21394.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1218743.

Phylogenomic databases

ProtClustDBCLSK862333.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-2941.

Family and domain databases

InterProIPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_ferredoxin-type.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001041. Ferredoxin.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR008333. OxRdtase_FAD-bd_dom.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR001221. Phe_hydroxylase.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
PfamPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMSSF54292. Ferredoxin. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.
PROSITEPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYLA_PSEPU
AccessionPrimary (citable) accession number: P21394
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: January 25, 2012
This is version 80 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