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Protein

Toluate 1,2-dioxygenase electron transfer component

Gene

xylZ

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Electron transfer component of toluate 1,2-dioxygenase system.

Catalytic activityi

Reduced ferredoxin + NAD+ = oxidized ferredoxin + NADH.

Cofactori

Protein has several cofactor binding sites:
  • FADBy similarity
  • [2Fe-2S] clusterBy similarityNote: Binds 1 [2Fe-2S] cluster per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi40Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi45Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi48Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation1
Metal bindingi81Iron-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-2963.

Names & Taxonomyi

Protein namesi
Recommended name:
Toluate 1,2-dioxygenase electron transfer component
Including the following 2 domains:
Ferredoxin
Ferredoxin--NAD(+) reductase (EC:1.18.1.3)
Gene namesi
Name:xylZ
Encoded oniPlasmid TOL pWW00 Publication
OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
Taxonomic identifieri303 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001676591 – 336Toluate 1,2-dioxygenase electron transfer componentAdd BLAST336

Interactioni

Subunit structurei

This dioxygenase system consists of three proteins: the two subunits of the hydroxylase component (XylX and XylY), and an electron transfer component (XylZ).

Structurei

3D structure databases

ProteinModelPortaliP23101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 972Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd BLAST95
Domaini104 – 204FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST101

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 336Ferredoxin-reductaseAdd BLAST238

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.

P23101-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHKVATDFE DGVTRFIDAN TGETVADAAY RQGINLPLDC RDGACGACKC
60 70 80 90 100
FAESGRYSLG EEYIEDALSE AEAEQGYVLT CQMRAESDCV IRVPAASDVC
110 120 130 140 150
KTQQAGYQAA ISNVRQLSES TIALSIKSAS LNQLAFLPGQ YVNLQVPGSD
160 170 180 190 200
QTRAYSFSSL QKDGEVSFLI RKLPGGLMSS FLTSLAKVGD SVSLAGPLGA
210 220 230 240 250
FYLREIKRPL LLLAGGTGLA PFTAMLEKIA EQGGEHPLHL IYGVTHDHDL
260 270 280 290 300
VEMDKLEAFA ARIPNFSYSA CVASPDSAYP QKGYVTQYIE PKQLNGGEVD
310 320 330
IYLCGPPPMV EAVSQYIRAQ GIQPANFYYE KFAASA
Length:336
Mass (Da):36,220
Last modified:November 1, 1991 - v1
Checksum:i2E74B6A2E2757CAB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64747 Genomic DNA. Translation: AAA26049.1.
PIRiC41659.
RefSeqiNP_542869.1. NC_003350.1.
WP_011005912.1. NC_003350.1.

Genome annotation databases

GeneIDi1218764.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64747 Genomic DNA. Translation: AAA26049.1.
PIRiC41659.
RefSeqiNP_542869.1. NC_003350.1.
WP_011005912.1. NC_003350.1.

3D structure databases

ProteinModelPortaliP23101.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1218764.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-2963.

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 nameiXYLZ_PSEPU
AccessioniPrimary (citable) accession number: P23101
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: November 30, 2016
This is version 91 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

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.