CNBZ_COMTE
ID CNBZ_COMTE Reviewed; 251 AA.
AC Q09KQ6;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=2-amino-5-chloromuconate deaminase {ECO:0000303|PubMed:16517619};
DE Short=2A5CM deaminase {ECO:0000303|PubMed:16517619};
DE AltName: Full=2-aminomuconate deaminase (2-hydroxymuconate-forming) {ECO:0000303|PubMed:17259310};
DE EC=3.5.99.11 {ECO:0000269|PubMed:16517619, ECO:0000269|PubMed:17259310};
GN Name=cnbZ {ECO:0000303|PubMed:17259310};
GN Synonyms=cnbH {ECO:0000303|PubMed:16517619};
OS Comamonas testosteroni (Pseudomonas testosteroni).
OG Plasmid pCNB1 {ECO:0000312|EMBL:ABI49649.1}.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=285;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CNB-1; PLASMID=pCNB1 {ECO:0000312|EMBL:ABM06247.1};
RX PubMed=15580337; DOI=10.1007/s00203-004-0738-5;
RA Wu J.F., Sun C.W., Jiang C.Y., Liu Z.P., Liu S.J.;
RT "A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-
RT chloronitrobenzene by Comamonas strain CNB-1: purification, properties,
RT genetic cloning and expression in Escherichia coli.";
RL Arch. Microbiol. 183:1-8(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=CNB-1; PLASMID=pCNB1 {ECO:0000312|EMBL:ABM06247.1};
RX PubMed=16517619; DOI=10.1128/aem.72.3.1759-1765.2006;
RA Wu J.F., Jiang C.Y., Wang B.J., Ma Y.F., Liu Z.P., Liu S.J.;
RT "Novel partial reductive pathway for 4-chloronitrobenzene and nitrobenzene
RT degradation in Comamonas sp. strain CNB-1.";
RL Appl. Environ. Microbiol. 72:1759-1765(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CNB-1; PLASMID=pCNB1 {ECO:0000312|EMBL:ABM06247.1};
RX PubMed=17526790; DOI=10.1128/aem.00616-07;
RA Ma Y.F., Wu J.F., Wang S.Y., Jiang C.Y., Zhang Y., Qi S.W., Liu L.,
RA Zhao G.P., Liu S.J.;
RT "Nucleotide sequence of plasmid pCNB1 from Comamonas strain CNB-1 reveals
RT novel genetic organization and evolution for 4-chloronitrobenzene
RT degradation.";
RL Appl. Environ. Microbiol. 73:4477-4483(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-9, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP INDUCTION, PATHWAY, AND SUBUNIT.
RC STRAIN=CNB-1 {ECO:0000312|EMBL:ABI49649.1};
RC PLASMID=pCNB1 {ECO:0000312|EMBL:ABI49649.1};
RX PubMed=17259310; DOI=10.1128/jb.01762-06;
RA Liu L., Wu J.F., Ma Y.F., Wang S.Y., Zhao G.P., Liu S.J.;
RT "A novel deaminase involved in chloronitrobenzene and nitrobenzene
RT degradation with Comamonas sp. strain CNB-1.";
RL J. Bacteriol. 189:2677-2682(2007).
CC -!- FUNCTION: Involved in the biodegradation of xenobiotic compounds, such
CC as nitrobenzene and 4-chloronitrobenzene (4-CNB) (PubMed:16517619).
CC CnbZ preferentially catalyzes the deamination of 2-amino-5-
CC chloromuconate (2A5CM) to yield 2-hydroxy-5-chloromuconate (2H5CM).
CC Also able to catalyze the deamination of 2-aminomuconate to yield 2-
CC hydroxymuconate, which spontaneously converts into its keto form, 2-
CC oxalocrotonate. {ECO:0000269|PubMed:16517619,
CC ECO:0000269|PubMed:17259310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,4E)-2-aminomuconate + H2O = (2Z,4E)-2-hydroxyhexa-2,4-
CC dienedioate + NH4(+); Xref=Rhea:RHEA:49460, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28080, ChEBI:CHEBI:28938, ChEBI:CHEBI:77859;
CC EC=3.5.99.11; Evidence={ECO:0000269|PubMed:16517619,
CC ECO:0000269|PubMed:17259310};
CC -!- ACTIVITY REGULATION: Cysteine residue modifying agents such as p-
CC chloromercuribenzoate and the SH-binding metals Zn(2+), Ni(2+) and
CC Cu(2+) completely inhibit deaminase activity, whereas Ca(2+), Mg(2+)
CC and the histidine residue-modifying agent diethyl pyrocarbonate inhibit
CC the activity by 23 to 50%. {ECO:0000269|PubMed:17259310}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 uM for 2-amino-5-chloromuconate {ECO:0000269|PubMed:17259310};
CC KM=8.8 uM for 2-aminomuconate {ECO:0000269|PubMed:17259310};
CC Vmax=196 umol/min/mg enzyme for 2-amino-5-chloromuconate as substrate
CC {ECO:0000269|PubMed:17259310};
CC Vmax=147 umol/min/mg enzyme for 2-aminomuconate as substrate
CC {ECO:0000269|PubMed:17259310};
CC -!- PATHWAY: Xenobiotic degradation; 4-chloronitrobenzene degradation.
CC {ECO:0000269|PubMed:16517619}.
CC -!- PATHWAY: Xenobiotic degradation; nitrobenzene degradation.
CC {ECO:0000269|PubMed:16517619}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17259310}.
CC -!- INDUCTION: By 4-chloronitrobenzene. {ECO:0000269|PubMed:17259310}.
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DR EMBL; EF079106; ABM06247.1; -; Genomic_DNA.
DR EMBL; DQ875599; ABI49649.1; -; Genomic_DNA.
DR RefSeq; YP_001967725.1; NC_010935.1.
DR AlphaFoldDB; Q09KQ6; -.
DR KEGG; ag:ABI49649; -.
DR PATRIC; fig|688245.4.peg.85; -.
DR UniPathway; UPA00923; -.
DR UniPathway; UPA01033; -.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IDA:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Direct protein sequencing; Hydrolase;
KW Plasmid.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17259310"
FT CHAIN 2..251
FT /note="2-amino-5-chloromuconate deaminase"
FT /id="PRO_0000442204"
SQ SEQUENCE 251 AA; 27648 MW; 5C6CDAA745552530 CRC64;
MPDAVVFSPG GYRYIPAVFQ YSAGIAAEPG FEIERVRFHR PVPLAEAFVA VESHLRAIGR
PTTSFAQCEL RSPDPFNDQG FIDFNTEYVK TLERWGIYKD RVNPVARTNV CPMYDKPTTP
SMFAFSYTVP TTSAAKRPSF QLAGGGDARG GSAPYKDRIV AFGDTSPEGL REKVVFVIEE
MESRLKTLGL GWADAVSTQL YTVQNIGHLV GPELARRGCG AGGLVWNYTR PPVIGLEYEM
DVRGAVRETV L
