ATZA_PSESD
ID ATZA_PSESD Reviewed; 474 AA.
AC P72156; Q79BR5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Atrazine chlorohydrolase {ECO:0000303|PubMed:7574646};
DE EC=3.8.1.8 {ECO:0000269|PubMed:22768133, ECO:0000269|PubMed:8759853};
GN Name=atzA {ECO:0000303|PubMed:8759853};
OS Pseudomonas sp. (strain ADP).
OG Plasmid pADP-1.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=47660;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RX PubMed=7574646; DOI=10.1128/aem.61.9.3373-3378.1995;
RA de Souza M.L., Wackett L.P., Boundy-Mills K.L., Mandelbaum R.T.,
RA Sadowsky M.J.;
RT "Cloning, characterization, and expression of a gene region from
RT Pseudomonas sp. strain ADP involved in the dechlorination of atrazine.";
RL Appl. Environ. Microbiol. 61:3373-3378(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8759853; DOI=10.1128/jb.178.16.4894-4900.1996;
RA de Souza M.L., Sadowsky M.J., Wackett L.P.;
RT "Atrazine chlorohydrolase from Pseudomonas sp. strain ADP: gene sequence,
RT enzyme purification, and protein characterization.";
RL J. Bacteriol. 178:4894-4900(1996).
RN [3]
RP SEQUENCE REVISION TO 335 AND 400-406.
RA de Souza M.L., Sadowsky M.J., Wackett L.P.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP ACTIVITY REGULATION, AND SIMILARITY WITH TRIA.
RC STRAIN=NRRL B-12227;
RX PubMed=11274097; DOI=10.1128/jb.183.8.2405-2410.2001;
RA Seffernick J.L., de Souza M.L., Sadowsky M.J., Wackett L.P.;
RT "Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but
RT functionally different.";
RL J. Bacteriol. 183:2405-2410(2001).
RN [5]
RP CHARACTERIZATION OF METAL REQUIREMENT, AND COFACTOR.
RX PubMed=12450410; DOI=10.1021/bi020415s;
RA Seffernick J.L., McTavish H., Osborne J.P., de Souza M.L., Sadowsky M.J.,
RA Wackett L.P.;
RT "Atrazine chlorohydrolase from Pseudomonas sp. strain ADP is a
RT metalloenzyme.";
RL Biochemistry 41:14430-14437(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PHE-84; ASN-328 AND
RP SER-331.
RX PubMed=22768133; DOI=10.1371/journal.pone.0039822;
RA Noor S., Taylor M.C., Russell R.J., Jermiin L.S., Jackson C.J.,
RA Oakeshott J.G., Scott C.;
RT "Intramolecular epistasis and the evolution of a new enzymatic function.";
RL PLoS ONE 7:E39822-E39822(2012).
RN [7] {ECO:0007744|PDB:4V1X, ECO:0007744|PDB:4V1Y}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH IRON, COFACTOR, AND
RP SUBUNIT.
RX PubMed=25760618; DOI=10.1107/s1399004715000619;
RA Peat T.S., Newman J., Balotra S., Lucent D., Warden A.C., Scott C.;
RT "The structure of the hexameric atrazine chlorohydrolase AtzA.";
RL Acta Crystallogr. D 71:710-720(2015).
CC -!- FUNCTION: Hydrolytically dechlorinates atrazine to hydroxyatrazine.
CC Dechlorinates also simazine, and desethylatrazine but is not active
CC with terbutylazine or desethyldesisopropylatrazine (PubMed:8759853).
CC Has no deaminase activity with melamine (PubMed:8759853,
CC PubMed:22768133). {ECO:0000269|PubMed:22768133,
CC ECO:0000269|PubMed:8759853}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=atrazine + H2O = chloride + H(+) + hydroxyatrazine;
CC Xref=Rhea:RHEA:11312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15930, ChEBI:CHEBI:17996, ChEBI:CHEBI:18316; EC=3.8.1.8;
CC Evidence={ECO:0000269|PubMed:22768133, ECO:0000269|PubMed:8759853};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:12450410, ECO:0000269|PubMed:25760618};
CC Note=Binds 1 Fe(2+) ion per subunit (PubMed:12450410, PubMed:25760618).
CC In vitro can also use Co(2+) or Mn(2+) (PubMed:12450410).
CC {ECO:0000269|PubMed:12450410, ECO:0000269|PubMed:25760618};
CC -!- ACTIVITY REGULATION: Atrazine dechlorination rates are reduced by
CC aminoatrazine but dechlorination is not inhibited by either melanine or
CC CAAT (2-chloro-4,6-diamino-s-triazine). {ECO:0000269|PubMed:11274097}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=149 uM for atrazine {ECO:0000269|PubMed:8759853};
CC Vmax=2.6 umol/min/mg enzyme {ECO:0000269|PubMed:8759853};
CC Note=kcat is 11 sec(-1) with atrazine as substrate.
CC {ECO:0000269|PubMed:8759853};
CC -!- PATHWAY: Xenobiotic degradation; atrazine degradation; cyanurate from
CC atrazine: step 1/3. {ECO:0000305|PubMed:7574646}.
CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000269|PubMed:25760618}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: AtzA and melamine deaminase (TriA) from Acidovorax
CC citrulli strain NRRL B-12227 are 98% identical but catalyze distinct
CC biochemical reactions. Enzymes differ by only 9 amino acids. These 9
CC amino acid differences between TriA and AtzA represent a short
CC evolutionary pathway connecting enzymes catalyzing physiologically
CC relevant deamination and dehalogenation reactions, respectively
CC (PubMed:11274097). Potential evolutionary trajectories between AtzA and
CC TriA have been constructed, and catalytic activities of the
CC intermediates along those trajectories have been characterized
CC (PubMed:22768133). {ECO:0000269|PubMed:22768133,
CC ECO:0000305|PubMed:11274097}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC ATZ/TRZ family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U66917; AAK50270.1; -; Genomic_DNA.
DR EMBL; U55933; AAC64663.1; -; Genomic_DNA.
DR PIR; T47197; T47197.
DR RefSeq; NP_862474.1; NC_004956.1.
DR RefSeq; WP_011117157.1; NC_004956.1.
DR PDB; 4V1X; X-ray; 2.20 A; A/B/C/D/E/F=1-474.
DR PDB; 4V1Y; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L=1-474.
DR PDBsum; 4V1X; -.
DR PDBsum; 4V1Y; -.
DR AlphaFoldDB; P72156; -.
DR SMR; P72156; -.
DR KEGG; ag:AAC64663; -.
DR BioCyc; MetaCyc:MON-901; -.
DR BRENDA; 3.8.1.8; 5085.
DR UniPathway; UPA00008; UER00499.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018788; F:atrazine chlorohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
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; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase; Iron;
KW Metal-binding; Plasmid.
FT CHAIN 1..474
FT /note="Atrazine chlorohydrolase"
FT /id="PRO_0000122293"
FT BINDING 66
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25760618,
FT ECO:0007744|PDB:4V1Y"
FT BINDING 68
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25760618,
FT ECO:0007744|PDB:4V1Y"
FT BINDING 276
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25760618,
FT ECO:0007744|PDB:4V1Y"
FT BINDING 327
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:25760618,
FT ECO:0007744|PDB:4V1Y"
FT SITE 84
FT /note="Major determinant of atrazine specificity"
FT /evidence="ECO:0000305|PubMed:22768133"
FT SITE 328
FT /note="Major determinant of atrazine specificity"
FT /evidence="ECO:0000305|PubMed:22768133"
FT SITE 331
FT /note="Major determinant of atrazine specificity"
FT /evidence="ECO:0000305|PubMed:22768133"
FT MUTAGEN 84
FT /note="F->L: 6.1-fold decrease in catalytic efficiency with
FT atrazine. Does not confer melamine deaminase activity.
FT 28.5-fold decrease in catalytic efficiency with atrazine
FT and strong increase in melanine deaminase activity; when
FT associated with D-328 and C-331."
FT /evidence="ECO:0000269|PubMed:22768133"
FT MUTAGEN 328
FT /note="N->D: 24.3-fold decrease in catalytic efficiency
FT with atrazine. Does not confer melamine deaminase activity.
FT 28.5-fold decrease in catalytic efficiency with atrazine
FT and strong increase in melanine deaminase activity; when
FT associated with L-84 and C-331."
FT /evidence="ECO:0000269|PubMed:22768133"
FT MUTAGEN 331
FT /note="S->C: 4.6-fold decrease in catalytic efficiency with
FT atrazine. Confers weak melamine deaminase activity. 28.5-
FT fold decrease in catalytic efficiency with atrazine and
FT strong increase in melanine deaminase activity; when
FT associated with L-84 and D-328."
FT /evidence="ECO:0000269|PubMed:22768133"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 20..29
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4V1X"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 70..74
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 101..117
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:4V1X"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 165..173
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:4V1X"
FT TURN 202..208
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:4V1X"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:4V1X"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 258..264
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 299..304
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 337..352
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 369..374
FT /evidence="ECO:0007829|PDB:4V1X"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 392..395
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 408..414
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:4V1X"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:4V1X"
FT HELIX 442..462
FT /evidence="ECO:0007829|PDB:4V1X"
SQ SEQUENCE 474 AA; 52486 MW; 51C1F6C755F141D4 CRC64;
MQTLSIQHGT LVTMDQYRRV LGDSWVHVQD GRIVALGVHA ESVPPPADRV IDARGKVVLP
GFINAHTHVN QILLRGGPSH GRQFYDWLFN VVYPGQKAMR PEDVAVAVRL YCAEAVRSGI
TTINENADSA IYPGNIEAAM AVYGEVGVRV VYARMFFDRM DGRIQGYVDA LKARSPQVEL
CSIMEETAVA KDRITALSDQ YHGTAGGRIS VWPAPATTTA VTVEGMRWAQ AFARDRAVMW
TLHMAESDHD ERIHGMSPAE YMECYGLLDE RLQVAHCVYF DRKDVRLLHR HNVKVASQVV
SNAYLGSGVA PVPEMVERGM AVGIGTDNGN SNDSVNMIGD MKFMAHIHRA VHRDADVLTP
EKILEMATID GARSLGMDHE IGSIETGKRA DLILLDLRHP QTTPHHHLAA TIVFQAYGNE
VDTVLIDGNV VMENRRLSFL PPERELAFLE EAQSRATAIL QRANMVANPA WRSL
