ATZE_PSESD
ID ATZE_PSESD Reviewed; 457 AA.
AC Q936X3;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=1-carboxybiuret hydrolase subunit AtzE {ECO:0000303|PubMed:29523689};
DE EC=3.5.1.131 {ECO:0000269|PubMed:29523689};
GN Name=atzE {ECO:0000303|PubMed:11544232};
OS Pseudomonas sp. (strain ADP).
OG Plasmid pADP-1.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=47660;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY, 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 X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ATZG, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29523689; DOI=10.1074/jbc.ra118.001996;
RA Esquirol L., Peat T.S., Wilding M., Liu J.W., French N.G., Hartley C.J.,
RA Onagi H., Nebl T., Easton C.J., Newman J., Scott C.;
RT "An unexpected vestigial protein complex reveals the evolutionary origins
RT of an s-triazine catabolic enzyme.";
RL J. Biol. Chem. 293:7880-7891(2018).
CC -!- FUNCTION: Hydrolyzes 1-carboxybiuret to urea-1,3-dicarboxylate and
CC NH(3). {ECO:0000269|PubMed:29523689}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-carboxybiuret + H2O = NH4(+) + urea-1,3-dicarboxylate;
CC Xref=Rhea:RHEA:58900, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:142864, ChEBI:CHEBI:142865; EC=3.5.1.131;
CC Evidence={ECO:0000269|PubMed:29523689};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for 1-carboxybiuret {ECO:0000269|PubMed:29523689};
CC KM=785 uM for 1-nitrobiuret {ECO:0000269|PubMed:29523689};
CC KM=167 uM for 1-carboxymalonamide {ECO:0000269|PubMed:29523689};
CC KM=523 uM for succinamate {ECO:0000269|PubMed:29523689};
CC Note=kcat is 15.5 sec(-1) with 1-carboxybiuret as substrate. kcat is
CC 9.4 sec(-1) with 1-nitrobiuret as substrate. kcat is 7 sec(-1) with
CC 1-carboxymalonamide as substrate. kcat is 19 sec(-1) with succinamate
CC as substrate. {ECO:0000269|PubMed:29523689};
CC -!- PATHWAY: Xenobiotic degradation; atrazine degradation.
CC {ECO:0000269|PubMed:11544232}.
CC -!- SUBUNIT: Heterotetramer consisting of 2 AtzE and 2 AtzG subunits.
CC {ECO:0000269|PubMed:29523689}.
CC -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to use biuret as substrate
CC (PubMed:11544232). But new evidence has shown that 1-carboxybiuret is
CC the real substrate. The error occurred since 1-carboxybiuret hydrolyzes
CC spontaneously to biuret (PubMed:29523689).
CC {ECO:0000269|PubMed:11544232, ECO:0000269|PubMed:29523689}.
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DR EMBL; U66917; AAK50332.1; -; Genomic_DNA.
DR RefSeq; NP_862538.1; NC_004956.1.
DR RefSeq; WP_011117192.1; NC_004956.1.
DR PDB; 6C62; X-ray; 1.95 A; A/B=1-457.
DR PDB; 6C6G; X-ray; 2.10 A; A/B=1-457.
DR PDBsum; 6C62; -.
DR PDBsum; 6C6G; -.
DR AlphaFoldDB; Q936X3; -.
DR SMR; Q936X3; -.
DR KEGG; ag:AAK50332; -.
DR BioCyc; MetaCyc:MON-13538; -.
DR BRENDA; 3.5.1.131; 14885.
DR UniPathway; UPA00008; -.
DR GO; GO:0018750; F:biuret amidohydrolase activity; IDA:UniProtKB.
DR GO; GO:0019381; P:atrazine catabolic process; IDA:UniProtKB.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR000120; Amidase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR014087; Carboxybiuret_hydro_AtzE.
DR PANTHER; PTHR11895; PTHR11895; 1.
DR Pfam; PF01425; Amidase; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR02715; amido_AtzE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Plasmid.
FT CHAIN 1..457
FT /note="1-carboxybiuret hydrolase subunit AtzE"
FT /id="PRO_0000418774"
FT ACT_SITE 74
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 174
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 17..35
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 43..58
FT /evidence="ECO:0007829|PDB:6C62"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 102..109
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:6C62"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 152..159
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:6C62"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 294..312
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6C62"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 340..360
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 365..375
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 389..392
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 393..396
FT /evidence="ECO:0007829|PDB:6C62"
FT TURN 397..401
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 402..407
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:6C62"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:6C6G"
FT STRAND 426..432
FT /evidence="ECO:0007829|PDB:6C62"
FT HELIX 437..449
FT /evidence="ECO:0007829|PDB:6C62"
SQ SEQUENCE 457 AA; 48120 MW; 68C88EA980DB7119 CRC64;
MKTVEIIEGI ASGRTSARDV CEEALATIGA TDGLINAFTC RTVERARAEA DAIDVRRARG
EVLPPLAGLP YAVKNLFDIE GVTTLAGSKI NRTLPPARAD AVLVQRLKAA GAVLLGGLNM
DEFAYGFTTE NTHYGPTRNP HDTGRIAGGS SGGSGAAIAA GQVPLSLGSD TNGSIRVPAS
LCGVWGLKPT FGRLSRRGTY PFVHSIDHLG PLADSVEGLA LAYDAMQGPD PLDPGCSASR
IQPSVPVLSQ GIAGLRIGVL GGWFRDNAGP AARAAVDVAA LTLGASEVVM WPDAEIGRAA
AFVITASEGG CLHLDDLRIR PQDFEPLSVD RFISGVLQPV AWYLRAQRFR RVYRDKVNAL
FRDWDILIAP ATPISAPAIG TEWIEVNGTR HPCRPAMGLL TQPVSFAGCP VVAAPTWPGE
NDGMPIGVQL IAAPWNESLC LRAGKVLQDT GIARLKC
