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Protein

Xylene monooxygenase electron transfer component

Gene

xylA

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi52Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi57Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi60Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi92Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2941.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylene monooxygenase electron transfer component
Including the following 2 domains:
Ferredoxin
Ferredoxin--NAD(+) reductase (EC:1.18.1.3)
Gene namesi
Name:xylA
Encoded oniPlasmid TOL pWW00 Publication
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001676601 – 350Xylene monooxygenase electron transfer componentAdd BLAST350

Proteomic databases

PRIDEiP21394.

Interactioni

Subunit structurei

Composed of two subunits: XylA and XylM.

Structurei

3D structure databases

ProteinModelPortaliP21394.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 1082Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST93
Domaini114 – 213FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST100

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni109 – 350Ferredoxin--NADH reductaseAdd BLAST242

Sequence similaritiesi

Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding FR-type domain.PROSITE-ProRule annotation

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21394-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEFFKKISG LFVPPPESTV SVRGQGFQFK VPRGQTILES ALHQGIAFPH
60 70 80 90 100
DCKVGSCGTC KYKLISGRVN ELTSSAMGLS GDLYQSGYRL GCQCIPKEDL
110 120 130 140 150
EIELDTVLGQ ALVPIETSAL ISKQKRLAHD IVEMEVVPDK QIAFYPGQYA
160 170 180 190 200
DVECAECSAV RSYSFSAPPQ PDGSLSFHVR LVPGGVFSGW LFGGDRTGAT
210 220 230 240 250
LTLRAPYGQF GLHESNATMV CVAGGTGLAP IKCVLQSMTQ AQRERDVLLF
260 270 280 290 300
FGARQQRDLY CLDEIEALQL DWGGRFELIP VLSEESSTSS WKGKRGMVTE
310 320 330 340 350
YFKEYLTGQP YEGYLCGPPP MVDAAETELV RLGVARELVF ADRFYNRPPC
Length:350
Mass (Da):38,455
Last modified:May 1, 1991 - v1
Checksum:i26828AC2226C1DDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37480 Genomic DNA. Translation: AAA26027.1.
D63341 Genomic DNA. Translation: BAA09663.1.
PIRiB37316.
RefSeqiNP_542886.1. NC_003350.1.
WP_011005929.1. NC_003350.1.

Genome annotation databases

GeneIDi1218743.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M37480 Genomic DNA. Translation: AAA26027.1.
D63341 Genomic DNA. Translation: BAA09663.1.
PIRiB37316.
RefSeqiNP_542886.1. NC_003350.1.
WP_011005929.1. NC_003350.1.

3D structure databases

ProteinModelPortaliP21394.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP21394.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1218743.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2941.

Family and domain databases

CDDicd00207. fer2. 1 hit.
Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR012675. Beta-grasp_dom.
IPR017927. Fd_Rdtase_FAD-bd.
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]
PfamiPF00970. FAD_binding_6. 1 hit.
PF00111. Fer2. 1 hit.
PF00175. NAD_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00371. FPNCR.
PR00410. PHEHYDRXLASE.
SUPFAMiSSF54292. SSF54292. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51384. FAD_FR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYLA_PSEPU
AccessioniPrimary (citable) accession number: P21394
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 30, 2016
This is version 96 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

Direct protein sequencing, Plasmid

Documents

  1. 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.