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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

Pathwayi: atrazine 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)DescriptionActionsGraphical viewLength
ChainiPRO_00000647611 – 363Cyanuric acid amidohydrolaseAdd BLAST363

Interactioni

Subunit structurei

Homotetramer.By similarity

Structurei

Secondary structure

1363
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 10Combined sources9
Helixi18 – 25Combined sources8
Helixi31 – 33Combined sources3
Beta strandi34 – 43Combined sources10
Helixi51 – 67Combined sources17
Helixi71 – 77Combined sources7
Beta strandi78 – 84Combined sources7
Beta strandi93 – 101Combined sources9
Beta strandi112 – 119Combined sources8
Helixi125 – 127Combined sources3
Helixi131 – 148Combined sources18
Helixi153 – 155Combined sources3
Beta strandi156 – 163Combined sources8
Helixi168 – 176Combined sources9
Helixi186 – 204Combined sources19
Helixi210 – 212Combined sources3
Helixi215 – 217Combined sources3
Turni218 – 220Combined sources3
Beta strandi226 – 233Combined sources8
Beta strandi241 – 248Combined sources8
Beta strandi254 – 264Combined sources11
Helixi268 – 277Combined sources10
Helixi283 – 288Combined sources6
Beta strandi289 – 296Combined sources8
Beta strandi302 – 304Combined sources3
Turni311 – 313Combined sources3
Beta strandi315 – 317Combined sources3
Helixi319 – 335Combined sources17
Beta strandi336 – 338Combined sources3
Beta strandi340 – 344Combined sources5
Beta strandi349 – 351Combined sources3
Beta strandi355 – 362Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BVQX-ray1.90A/B1-363[»]
4BVRX-ray2.58A/B1-363[»]
4BVSX-ray2.60A/B1-363[»]
4BVTX-ray3.10A/B1-363[»]
SMRiP58329.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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. NZ_CM003636.1.

Genome annotation databases

GeneIDi1440634.

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. NZ_CM003636.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4BVQX-ray1.90A/B1-363[»]
4BVRX-ray2.58A/B1-363[»]
4BVSX-ray2.60A/B1-363[»]
4BVTX-ray3.10A/B1-363[»]
SMRiP58329.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1440634.

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...

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: November 30, 2016
This is version 46 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

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.