ATZF_PSESD
ID ATZF_PSESD Reviewed; 605 AA.
AC Q936X2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Allophanate hydrolase;
DE EC=3.5.1.54;
GN Name=atzF;
OS Pseudomonas sp. (strain ADP).
OG Plasmid pADP-1.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=47660;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND GENE NAME.
RC STRAIN=ADP;
RX PubMed=11544232; DOI=10.1128/jb.183.19.5684-5697.2001;
RA Martinez B., Tomkins J., Wackett L.P., Wing R., Sadowsky M.J.;
RT "Complete nucleotide sequence and organization of the atrazine catabolic
RT plasmid pADP-1 from Pseudomonas sp. strain ADP.";
RL J. Bacteriol. 183:5684-5697(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, SUBUNIT, AND MUTAGENESIS OF LYS-91; SER-165 AND
RP SER-189.
RC STRAIN=ADP;
RX PubMed=15901697; DOI=10.1128/jb.187.11.3731-3738.2005;
RA Shapir N., Sadowsky M.J., Wackett L.P.;
RT "Purification and characterization of allophanate hydrolase (AtzF) from
RT Pseudomonas sp. strain ADP.";
RL J. Bacteriol. 187:3731-3738(2005).
CC -!- FUNCTION: Hydrolyzes allophanate to NH(3) and CO(2). Can also use
CC malonamate, but with much lower efficiency.
CC {ECO:0000269|PubMed:11544232, ECO:0000269|PubMed:15901697}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H(+) + H2O + urea-1-carboxylate = 2 CO2 + 2 NH4(+);
CC Xref=Rhea:RHEA:19029, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15832, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.54;
CC Evidence={ECO:0000269|PubMed:11544232, ECO:0000269|PubMed:15901697};
CC -!- ACTIVITY REGULATION: Inhibited, in a time-dependent manner, by phenyl
CC phosphorodiamidate, which forms a covalently modified Ser-189.
CC {ECO:0000269|PubMed:15901697}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.5 mM for allophanate {ECO:0000269|PubMed:15901697};
CC KM=5.3 mM for malonamate {ECO:0000269|PubMed:15901697};
CC Note=kcat is 16.4 sec(-1) for allophanate. kcat is 0.1 sec(-1) for
CC malonamate.;
CC pH dependence:
CC Optimum pH is 9.5. {ECO:0000269|PubMed:15901697};
CC -!- PATHWAY: Xenobiotic degradation; atrazine degradation.
CC {ECO:0000269|PubMed:11544232, ECO:0000269|PubMed:15901697}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15901697}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR EMBL; U66917; AAK50333.1; -; Genomic_DNA.
DR RefSeq; NP_862539.1; NC_004956.1.
DR RefSeq; WP_011117193.1; NC_004956.1.
DR PDB; 4CP8; X-ray; 2.50 A; A/B/C/D/E/F=1-467.
DR PDBsum; 4CP8; -.
DR AlphaFoldDB; Q936X2; -.
DR SMR; Q936X2; -.
DR KEGG; ag:AAK50333; -.
DR BioCyc; MetaCyc:MON-13515; -.
DR BRENDA; 3.5.1.54; 5085.
DR UniPathway; UPA00008; -.
DR GO; GO:0004039; F:allophanate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0019381; P:atrazine catabolic process; IDA:UniProtKB.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR014085; Allophanate_hydrolase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR02713; allophanate_hyd; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Plasmid.
FT CHAIN 1..605
FT /note="Allophanate hydrolase"
FT /id="PRO_0000418775"
FT ACT_SITE 91
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 165
FT /note="Charge relay system"
FT /evidence="ECO:0000305"
FT ACT_SITE 189
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 91
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15901697"
FT MUTAGEN 165
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15901697"
FT MUTAGEN 189
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:15901697"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:4CP8"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:4CP8"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 179..188
FT /evidence="ECO:0007829|PDB:4CP8"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4CP8"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:4CP8"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 231..241
FT /evidence="ECO:0007829|PDB:4CP8"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 284..299
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 326..331
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 345..352
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 359..380
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 384..390
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 397..402
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 406..411
FT /evidence="ECO:0007829|PDB:4CP8"
FT TURN 412..422
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 423..432
FT /evidence="ECO:0007829|PDB:4CP8"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:4CP8"
FT HELIX 450..463
FT /evidence="ECO:0007829|PDB:4CP8"
SQ SEQUENCE 605 AA; 64060 MW; BD2F95218643BD00 CRC64;
MNDRAPHPER SGRVTPDHLT DLASYQAAYA AGTDAADVIS DLYARIKEDG ENPIWISLLP
LESALAMLAD AQQRKDKGEA LPLFGIPFGV KDNIDVAGLP TTAGCTGFAR TPRQHAFVVQ
RLVDAGAIPI GKTNLDQFAT GLNGTRTPFG IPRCVFNENY VSGGSSSGSA VAVANGTVPF
SLGTDTAGSG RIPAAFNNLV GLKPTKGLFS GSGLVPAARS LDCISVLAHT VDDALAVARV
AAGYDADDAF SRKAGAAALT EKSWPRRFNF GVPAAEHRQF FGDAEAEALF NKAVRKLEEM
GGTCISFDYT PFRQAAELLY AGPWVAERLA AIESLADEHP EVLHPVVRDI ILSAKRMSAV
DTFNGIYRLA DLVRAAESTW EKIDVMLLPT APTIYTVEDM LADPVRLNSN LGFYTNFVNL
MDLSAIAVPA GFRTNGLPFG VTFIGRAFED GAIASLGKAF VEHDLAKGNA ATAAPPKDTV
AIAVVGAHLS DQPLNHQLTE SGGKLRATTR TAPGYALYAL RDATPAKPGM LRDQNAVGSI
EVEIWDLPVA GFGAFVSEIP APLGIGTITL EDGSHVKGFL CEPHAIETAL DITHYGGWRA
YLAAQ
