P95442 (ATZB_PSESD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hydroxydechloroatrazine ethylaminohydrolase
Short name=Hydroxyatrazine hydrolase
EC=3.5.99.3

Gene names

Name:

atzB

Encoded on

Plasmid pADP-1

Organism

Pseudomonas sp. (strain ADP)

Taxonomic identifier

47660 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › unclassified Proteobacteria › unclassified pseudomonads

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the deamination reaction of hydroxyatrazine to N-isopropylammelide (dihydroxy-isopropyl-atrazine). The enzyme is also capable of catalyzing some dechlorinating reactions. Ref.2
Catalytic activity	4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H2O = N-isopropylammelide + ethylamine. Ref.2
Cofactor	Binds 1 zinc ion per subunit. Ref.2
Pathway	Xenobiotic degradation; atrazine degradation; cyanurate from atrazine: step 2/3.
Subunit structure	Homodimer. Ref.2
Subcellular location	Cytoplasm Potential.
Sequence similarities	Belongs to the ATZ/TRZ family.
Biophysicochemical properties	Kinetic parameters: KM=20 µM for hydroxyatrazine Ref.2 KM=40 µM for 6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-triazine KM=29 µM for 2,4-diisopropylamino-6-hydroxy-1,3,5-triazine KM=120 µM for 2-chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine KM=230 µM for 2-chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine pH dependence: Optimum pH is 6.5-7.5.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Plasmid
Gene Ontology (GO)
Biological_process	atrazine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	hydroxydechloroatrazine ethylaminohydrolase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 481	481	Hydroxydechloroatrazine ethylaminohydrolase		PRO_0000122295
Sites
	Metal binding	74	1	Zinc; via tele nitrogen By similarity
	Metal binding	76	1	Zinc; via tele nitrogen By similarity
	Metal binding	245	1	Zinc; via tele nitrogen By similarity
	Metal binding	331	1	Zinc By similarity

Sequences

	Sequence		Length	Mass (Da)
	P95442 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: BF2EF1C5891CDA41	FASTA	481	52,113
	10 20 30 40 50 60 MTTTLYTGFH QLVTGDVAGT VLNGVDILVR DGEIIGLGPD LPRTLAPIGV GQEQGVEVVN 70 80 90 100 110 120 CRGLTAYPGL INTHHHFFQA FVRNLAPLDW TQLDVLAWLR KIYPVFALVD EDCIYHSTVV 130 140 150 160 170 180 SMAELIKHGC TTAFDHQYNY SRRGGPFLVD RQFDAANLLG LRFHAGRGCI TLPMAEGSTI 190 200 210 220 230 240 PDAMRESTDT FLADCERLVS RFHDPRPFAM QRVVVAPSSP VIAYPETFVE SARLARHLGV 250 260 270 280 290 300 SLHTHLGEGE TPAMVARFGE RSLDWCENRG FVGPDVWLAH GWEFTAADIA RLAATGTGVA 310 320 330 340 350 360 HCPAPVFLVG AEVTDIPAMA AAGVRVGFGV DGHASNDSSN LAECIRLAYL LQCLKASERQ 370 380 390 400 410 420 HPVPAPYDFL RMATQGGADC LNRPDLGALA VGRAADFFAV DLNRIEYIGA NHDPRSLPAK 430 440 450 460 470 480 VGFSGPVDMT VINGKVVWRN GEFPGLDEME LARAADGVFR RVIYGDPLVA ALRRGTGVTP C

References

[1]	"The atzB gene of Pseudomonas sp. strain ADP encodes the second enzyme of a novel atrazine degradation pathway." Boundy-Mills K.L., de Souza M.L., Mandelbaum R.T., Wackett L.P., Sadowsky M.J. Appl. Environ. Microbiol. 63:916-923(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase superfamily enzyme catalyzing deamination and dechlorination." Seffernick J.L., Aleem A., Osborne J.P., Johnson G., Sadowsky M.J., Wackett L.P. J. Bacteriol. 189:6989-6997(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U66917 Genomic DNA. Translation: AAC45138.1.
RefSeq	NP_862481.1. NC_004956.1.
3D structure databases
ProteinModelPortal	P95442.
ModBase	Search...
Proteomic databases
ProMEX	P95442.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1440579.
Phylogenomic databases
ProtClustDB	CLSK586607.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-902.
SABIO-RK	P95442.
UniPathway	UPA00008; UER00500.
Family and domain databases
InterPro	IPR006680. Amidohydro_1. IPR011059. Metal-dep_hydrolase_composite. [Graphical view]
Pfam	PF01979. Amidohydro_1. 1 hit. [Graphical view]
SUPFAM	SSF51338. Metalo_hydrolase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ATZB_PSESD

Accession

Primary (citable) accession number: P95442

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 1, 1997
Last modified:	April 3, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program