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Protein

Cyanuric acid amidohydrolase

Gene

atzD

Organism
Pseudomonas sp. (strain ADP)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for s-triazine ring cleavage. Cleaves cyanuric acid (2,4,6-trihydroxy-s-triazine) to yield carbon dioxide and biuret.1 Publication

Catalytic activityi

Cyanuric acid + H2O = biuret + CO2.1 Publication

Pathway:iatrazine degradation

This protein is involved in step 1 of the subpathway that synthesizes biuret from cyanurate.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Cyanuric acid amidohydrolase (atzD)
This subpathway is part of the pathway atrazine degradation, which is itself part of Xenobiotic degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes biuret from cyanurate, the pathway atrazine degradation and in Xenobiotic degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-13543.
BRENDAi3.5.2.15. 5085.
UniPathwayiUPA00008; UER00502.

Names & Taxonomyi

Protein namesi
Recommended name:
Cyanuric acid amidohydrolase (EC:3.5.2.15)
Gene namesi
Name:atzD
Encoded oniPlasmid pADP-10 Publication
OrganismiPseudomonas sp. (strain ADP)
Taxonomic identifieri47660 [NCBI]
Taxonomic lineageiBacteriaProteobacteria

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Cyanuric acid amidohydrolasePRO_0000064761Add
BLAST

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

Secondary structure

1
363
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 109Combined sources
Helixi18 – 258Combined sources
Helixi31 – 333Combined sources
Beta strandi34 – 4310Combined sources
Helixi51 – 6717Combined sources
Helixi71 – 777Combined sources
Beta strandi78 – 847Combined sources
Beta strandi93 – 1019Combined sources
Beta strandi112 – 1198Combined sources
Helixi125 – 1273Combined sources
Helixi131 – 14818Combined sources
Helixi153 – 1553Combined sources
Beta strandi156 – 1638Combined sources
Helixi168 – 1769Combined sources
Helixi186 – 20419Combined sources
Helixi210 – 2123Combined sources
Helixi215 – 2173Combined sources
Turni218 – 2203Combined sources
Beta strandi226 – 2338Combined sources
Beta strandi241 – 2488Combined sources
Beta strandi254 – 26411Combined sources
Helixi268 – 27710Combined sources
Helixi283 – 2886Combined sources
Beta strandi289 – 2968Combined sources
Beta strandi302 – 3043Combined sources
Turni311 – 3133Combined sources
Beta strandi315 – 3173Combined sources
Helixi319 – 33517Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi340 – 3445Combined sources
Beta strandi349 – 3513Combined sources
Beta strandi355 – 3628Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BVQX-ray1.90A/B1-363[»]
4BVRX-ray2.58A/B1-363[»]
4BVSX-ray2.60A/B1-363[»]
4BVTX-ray3.10A/B1-363[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

KOiK03383.

Family and domain databases

InterProiIPR014086. AtzD/Barbiturase.
[Graphical view]
PfamiPF09663. Amido_AtzD_TrzD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02714. amido_AtzD_TrzD. 1 hit.

Sequencei

Sequence statusi: Complete.

P58329-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYHIDVFRIP CHSPGDTSGL EDLIETGRVA PADIVAVMGK TEGNGCVNDY
60 70 80 90 100
TREYATAMLA ACLGRHLQLP PHEVEKRVAF VMSGGTEGVL SPHHTVFARR
110 120 130 140 150
PAIDAHRPAG KRLTLGIAFT RDFLPEEIGR HAQITETAGA VKRAMRDAGI
160 170 180 190 200
ASIDDLHFVQ VKCPLLTPAK IASARSRGCA PVTTDTYESM GYSRGASALG
210 220 230 240 250
IALATEEVPS SMLVDESVLN DWSLSSSLAS ASAGIELEHN VVIAIGMSEQ
260 270 280 290 300
ATSELVIAHG VMSDAIDAAS VRRTIESLGI RSDDEMDRIV NVFAKAEASP
310 320 330 340 350
DGVVRGMRHT MLSDSDINST RHARAVTGAA IASVVGHGMV YVSGGAEHQG
360
PAGGGPFAVI ARA
Length:363
Mass (Da):38,200
Last modified:October 24, 2001 - v1
Checksum:i140256C30D82FF83
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66917 Genomic DNA. Translation: AAK50331.1.
RefSeqiNP_862537.1. NC_004956.1.
WP_011117191.1. NG_041462.1.
YP_009089919.1. NG_041462.1.

Genome annotation databases

GeneIDi1440634.
KEGGipg:1440634.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66917 Genomic DNA. Translation: AAK50331.1.
RefSeqiNP_862537.1. NC_004956.1.
WP_011117191.1. NG_041462.1.
YP_009089919.1. NG_041462.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BVQX-ray1.90A/B1-363[»]
4BVRX-ray2.58A/B1-363[»]
4BVSX-ray2.60A/B1-363[»]
4BVTX-ray3.10A/B1-363[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1440634.
KEGGipg:1440634.

Phylogenomic databases

KOiK03383.

Enzyme and pathway databases

UniPathwayiUPA00008; UER00502.
BioCyciMetaCyc:MONOMER-13543.
BRENDAi3.5.2.15. 5085.

Family and domain databases

InterProiIPR014086. AtzD/Barbiturase.
[Graphical view]
PfamiPF09663. Amido_AtzD_TrzD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02714. amido_AtzD_TrzD. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete nucleotide sequence and organization of the atrazine catabolic plasmid pADP-1 from Pseudomonas sp. strain ADP."
    Martinez B., Tomkins J., Wackett L.P., Wing R., Sadowsky M.J.
    J. Bacteriol. 183:5684-5697(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    Strain: ADP.

Entry informationi

Entry nameiATZD_PSESD
AccessioniPrimary (citable) accession number: P58329
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2001
Last sequence update: October 24, 2001
Last modified: April 1, 2015
This is version 42 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, Plasmid

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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 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.