ID   ATZB_PSESD              Reviewed;         481 AA.
AC   P95442;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Hydroxydechloroatrazine ethylaminohydrolase;
DE            Short=Hydroxyatrazine hydrolase;
DE            EC=3.5.4.43 {ECO:0000269|PubMed:17660279};
GN   Name=atzB;
OS   Pseudomonas sp. (strain ADP).
OG   Plasmid pADP-1.
OC   Bacteria; Proteobacteria.
OX   NCBI_TaxID=47660;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9055410; DOI=10.1128/aem.63.3.916-923.1997;
RA   Boundy-Mills K.L., de Souza M.L., Mandelbaum R.T., Wackett L.P.,
RA   Sadowsky M.J.;
RT   "The atzB gene of Pseudomonas sp. strain ADP encodes the second enzyme of a
RT   novel atrazine degradation pathway.";
RL   Appl. Environ. Microbiol. 63:916-923(1997).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, COFACTOR, AND SUBUNIT.
RX   PubMed=17660279; DOI=10.1128/jb.00630-07;
RA   Seffernick J.L., Aleem A., Osborne J.P., Johnson G., Sadowsky M.J.,
RA   Wackett L.P.;
RT   "Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase
RT   superfamily enzyme catalyzing deamination and dechlorination.";
RL   J. Bacteriol. 189:6989-6997(2007).
CC   -!- FUNCTION: Catalyzes the deamination reaction of hydroxyatrazine to N-
CC       isopropylammelide (dihydroxy-isopropyl-atrazine). The enzyme is also
CC       capable of catalyzing some dechlorinating reactions.
CC       {ECO:0000269|PubMed:17660279}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + H2O + hydroxyatrazine = ethylamine + N-
CC         isopropylammelide; Xref=Rhea:RHEA:23092, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17247, ChEBI:CHEBI:18316,
CC         ChEBI:CHEBI:566789; EC=3.5.4.43;
CC         Evidence={ECO:0000269|PubMed:17660279};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:17660279};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17660279};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=20 uM for hydroxyatrazine {ECO:0000269|PubMed:17660279};
CC         KM=40 uM for 6-hydroxy-4-(N-isopropylamino)-2-(N-methylamino)-1,3,5-
CC         triazine {ECO:0000269|PubMed:17660279};
CC         KM=29 uM for 2,4-diisopropylamino-6-hydroxy-1,3,5-triazine
CC         {ECO:0000269|PubMed:17660279};
CC         KM=120 uM for 2-chloro-4-hydroxy-6-(N-isopropylamino)-1,3,5-triazine
CC         {ECO:0000269|PubMed:17660279};
CC         KM=230 uM for 2-chloro-4-(N-ethylamino)-6-hydroxy-1,3,5-triazine
CC         {ECO:0000269|PubMed:17660279};
CC       pH dependence:
CC         Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:17660279};
CC   -!- PATHWAY: Xenobiotic degradation; atrazine degradation; cyanurate from
CC       atrazine: step 2/3.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17660279}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       ATZ/TRZ family. {ECO:0000305}.
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DR   EMBL; U66917; AAC45138.1; -; Genomic_DNA.
DR   RefSeq; NP_862481.1; NC_004956.1.
DR   RefSeq; WP_011117160.1; NC_004956.1.
DR   AlphaFoldDB; P95442; -.
DR   SMR; P95442; -.
DR   PRIDE; P95442; -.
DR   KEGG; ag:AAC45138; -.
DR   BioCyc; MetaCyc:MON-902; -.
DR   SABIO-RK; P95442; -.
DR   UniPathway; UPA00008; UER00500.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0018763; F:hydroxydechloroatrazine ethylaminohydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019381; P:atrazine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; SSF51338; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Metal-binding; Plasmid; Zinc.
FT   CHAIN           1..481
FT                   /note="Hydroxydechloroatrazine ethylaminohydrolase"
FT                   /id="PRO_0000122295"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         76
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         245
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         331
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   481 AA;  52113 MW;  BF2EF1C5891CDA41 CRC64;
     MTTTLYTGFH QLVTGDVAGT VLNGVDILVR DGEIIGLGPD LPRTLAPIGV GQEQGVEVVN
     CRGLTAYPGL INTHHHFFQA FVRNLAPLDW TQLDVLAWLR KIYPVFALVD EDCIYHSTVV
     SMAELIKHGC TTAFDHQYNY SRRGGPFLVD RQFDAANLLG LRFHAGRGCI TLPMAEGSTI
     PDAMRESTDT FLADCERLVS RFHDPRPFAM QRVVVAPSSP VIAYPETFVE SARLARHLGV
     SLHTHLGEGE TPAMVARFGE RSLDWCENRG FVGPDVWLAH GWEFTAADIA RLAATGTGVA
     HCPAPVFLVG AEVTDIPAMA AAGVRVGFGV DGHASNDSSN LAECIRLAYL LQCLKASERQ
     HPVPAPYDFL RMATQGGADC LNRPDLGALA VGRAADFFAV DLNRIEYIGA NHDPRSLPAK
     VGFSGPVDMT VINGKVVWRN GEFPGLDEME LARAADGVFR RVIYGDPLVA ALRRGTGVTP
     C