ATZC_PSESD
ID ATZC_PSESD Reviewed; 403 AA.
AC O52063;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=N-isopropylammelide isopropyl amidohydrolase;
DE EC=3.5.4.42 {ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:26390431};
GN Name=atzC;
OS Pseudomonas sp. (strain ADP).
OG Plasmid pADP-1.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=47660;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9422605; DOI=10.1128/jb.180.1.152-158.1998;
RA Sadowsky M.J., Tong Z., de Souza M., Wackett L.P.;
RT "AtzC is a new member of the amidohydrolase protein superfamily and is
RT homologous to other atrazine-metabolizing enzymes.";
RL J. Bacteriol. 180:152-158(1998).
RN [2]
RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVITY
RP REGULATION, AND EPR SPECTROSCOPY.
RC STRAIN=ADP;
RX PubMed=12218024; DOI=10.1128/jb.184.19.5376-5384.2002;
RA Shapir N., Osborne J.P., Johnson G., Sadowsky M.J., Wackett L.P.;
RT "Purification, substrate range, and metal center of AtzC: the N-
RT isopropylammelide aminohydrolase involved in bacterial atrazine
RT metabolism.";
RL J. Bacteriol. 184:5376-5384(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) IN COMPLEX WITH ZINC, AND COFACTOR.
RC STRAIN=ADP;
RA Fedorov A.A., Fedorov E.V., Seffernick J., Wackett L.P., Burley S.K.,
RA Almo S.C.;
RT "Crystal structure of N-isopropylammelide isopropylaminohydrolase AtzC from
RT Pseudomonas sp. strain ADP complexed with Zn.";
RL Submitted (AUG-2007) to the PDB data bank.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH ZINC AND INHIBITOR
RP OF WILD-TYPE AND MUTANTS ALA-219; ALA-249 AND ASP-304, CATALYTIC ACTIVITY,
RP SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-65; GLN-160;
RP ASP-188; HIS-219; HIS-249; ASP-303; ASN-304 AND TRP-309, AND ACTIVE SITE.
RC STRAIN=ADP;
RX PubMed=26390431; DOI=10.1371/journal.pone.0137700;
RA Balotra S., Warden A.C., Newman J., Briggs L.J., Scott C., Peat T.S.;
RT "X-ray structure and mutagenesis studies of the N-isopropylammelide
RT isopropylaminohydrolase, AtzC.";
RL PLoS ONE 10:E0137700-E0137700(2015).
CC -!- FUNCTION: Transforms N-isopropylammelide to cyanuric acid and
CC isopropylamine. {ECO:0000269|PubMed:12218024,
CC ECO:0000269|PubMed:9422605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + H2O + N-isopropylammelide = cyanurate + isopropylamine;
CC Xref=Rhea:RHEA:23608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17247, ChEBI:CHEBI:38028, ChEBI:CHEBI:57492; EC=3.5.4.42;
CC Evidence={ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:26390431};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:12218024, ECO:0000269|PubMed:26390431,
CC ECO:0000269|Ref.3};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000269|PubMed:12218024,
CC ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylammeline, N-
CC hydroxyethylammeline, N-isopropylammeline, ammeline and 2-amino-
CC 4hydroxy-1,3,5-s-triazine. {ECO:0000269|PubMed:12218024}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=817 uM for N-methylammelide {ECO:0000269|PubMed:12218024};
CC KM=308 uM for N-ethylammelide {ECO:0000269|PubMed:12218024};
CC KM=3860 uM for N-hydroxyethylammelide {ECO:0000269|PubMed:12218024};
CC KM=406 uM for N-isopropylammelide {ECO:0000269|PubMed:12218024};
CC KM=580 uM for N-cyclopropylammelide {ECO:0000269|PubMed:12218024};
CC KM=299 uM for N-t-butylammelide {ECO:0000269|PubMed:12218024};
CC KM=155 uM for N-dimethylammelide {ECO:0000269|PubMed:12218024};
CC KM=1320 uM for ammelide {ECO:0000269|PubMed:12218024};
CC Note=kcat is 178 sec(-1) for N-methylammelide. kcat is 209 sec(-1)
CC for N-ethylammelide. kcat is 80.6 sec(-1) for N-hydroxyethylammelide.
CC kcat is 13.3 sec(-1) for N-isopropylammelide. kcat is 98.2 sec(-1)
CC for N-cyclopropylammelide. kcat is 0.07 sec(-1) for N-t-
CC butylammelide. kcat is 10.7 sec(-1) for N-dimethylammelide. kcat is
CC 1.65 sec(-1) for ammelide. {ECO:0000269|PubMed:12218024};
CC pH dependence:
CC Optimum pH is 7.25. {ECO:0000269|PubMed:26390431};
CC -!- PATHWAY: Xenobiotic degradation; atrazine degradation; cyanurate from
CC atrazine: step 3/3.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12218024,
CC ECO:0000269|PubMed:26390431}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. N-
CC acyl-D-amino-acid deacylase family. {ECO:0000305}.
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DR EMBL; U66917; AAB96621.1; -; Genomic_DNA.
DR RefSeq; NP_862508.1; NC_004956.1.
DR RefSeq; WP_011117177.1; NC_004956.1.
DR PDB; 2QT3; X-ray; 2.24 A; A/B=1-403.
DR PDB; 4CQB; X-ray; 1.84 A; A/B=1-403.
DR PDB; 4CQC; X-ray; 2.20 A; A/B=1-403.
DR PDB; 4CQD; X-ray; 2.25 A; A/B=1-403.
DR PDB; 5AKQ; X-ray; 2.60 A; A/B=1-403.
DR PDBsum; 2QT3; -.
DR PDBsum; 4CQB; -.
DR PDBsum; 4CQC; -.
DR PDBsum; 4CQD; -.
DR PDBsum; 5AKQ; -.
DR AlphaFoldDB; O52063; -.
DR SMR; O52063; -.
DR KEGG; ag:AAB96621; -.
DR BioCyc; MetaCyc:MON-921; -.
DR BRENDA; 3.5.4.42; 5085.
DR UniPathway; UPA00008; UER00501.
DR EvolutionaryTrace; O52063; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018764; F:N-isopropylammelide isopropylaminohydrolase activity; IEA:UniProtKB-EC.
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; Hydrolase; Metal-binding; Plasmid; Zinc.
FT CHAIN 1..403
FT /note="N-isopropylammelide isopropyl amidohydrolase"
FT /id="PRO_0000182707"
FT ACT_SITE 249
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:26390431"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3"
FT BINDING 217
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:26390431, ECO:0000269|Ref.3"
FT MUTAGEN 65
FT /note="K->A: 30-fold increase in kcat with ammelide as
FT substrate."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 65
FT /note="K->R: 12-fold increase in kcat with ammelide as
FT substrate."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 160
FT /note="Q->A,E: Almost no effect."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 188
FT /note="D->A: 5-fold increase in kcat with ammelide as
FT substrate."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 188
FT /note="D->N: No effect."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 219
FT /note="H->A: Almost no effect."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 249
FT /note="H->A: No activity."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 303
FT /note="D->A,N: Almost no effect."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 304
FT /note="N->A: Almost no effect."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 304
FT /note="N->D: 7-fold increase in kcat with ammelide as
FT substrate."
FT /evidence="ECO:0000269|PubMed:26390431"
FT MUTAGEN 309
FT /note="W->A,F: Almost no effect."
FT /evidence="ECO:0000269|PubMed:26390431"
FT STRAND 4..14
FT /evidence="ECO:0007829|PDB:4CQB"
FT TURN 15..18
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:4CQB"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:4CQB"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:4CQB"
FT TURN 130..134
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:4CQB"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:4CQB"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:4CQB"
FT TURN 189..193
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 222..238
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 245..249
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:4CQB"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 333..343
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 345..351
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 367..374
FT /evidence="ECO:0007829|PDB:4CQB"
FT HELIX 375..381
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:4CQB"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:4CQB"
SQ SEQUENCE 403 AA; 44938 MW; 0B91206B436EEC64 CRC64;
MSKDFDLIIR NAYLSEKDSV YDIGIVGDRI IKIEAKIEGT VKDEIDAKGN LVSPGFVDAH
THMDKSFTST GERLPKFWSR PYTRDAAIED GLKYYKNATH EEIKRHVIEH AHMQVLHGTL
YTRTHVDVDS VAKTKAVEAV LEAKEELKDL IDIQVVAFAQ SGFFVDLESE SLIRKSLDMG
CDLVGGVDPA TRENNVEGSL DLCFKLAKEY DVDIDYHIHD IGTVGVYSIN RLAQKTIENG
YKGRVTTSHA WCFADAPSEW LDEAIPLYKD SGMKFVTCFS STPPTMPVIK LLEAGINLGC
ASDNIRDFWV PFGNGDMVQG ALIETQRLEL KTNRDLGLIW KMITSEGARV LGIEKNYGIE
VGKKADLVVL NSLSPQWAII DQAKRLCVIK NGRIIVKDEV IVA
