ID   CNBH_COMTE              Reviewed;         462 AA.
AC   Q38M35;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=2-amino-5-chloromuconic acid deaminase {ECO:0000303|PubMed:16517619};
DE   AltName: Full=2-aminomuconate deaminase {ECO:0000303|PubMed:16517619};
DE            EC=3.5.99.5 {ECO:0000269|PubMed:16517619};
GN   Name=cnbH {ECO:0000303|PubMed:16517619};
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OG   Plasmid pCNB {ECO:0000312|EMBL:ABB13583.2}.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CNB-1; PLASMID=pCNB {ECO:0000312|EMBL:ABB13583.2};
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=pCNB {ECO:0000312|EMBL:ABB13583.2};
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=pCNB {ECO:0000312|EMBL:ABB13583.2};
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).
CC   -!- FUNCTION: Involved in the biodegradation of nitroaromatic and
CC       chlorinated nitroaromatic compounds. Catalyzes the conversion of 2-
CC       amino-5-chloromuconic acid into 2-hydroxy-5-chloromuconic acid and
CC       ammonia. Also able to catalyze the transformation of 2-aminomuconic
CC       acid into 2-hydroxymuconic acid. {ECO:0000269|PubMed:16517619}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2Z,4E)-2-aminomuconate + H2O = (3E)-2-oxohex-3-enedioate +
CC         NH4(+); Xref=Rhea:RHEA:20996, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:64908, ChEBI:CHEBI:77859; EC=3.5.99.5;
CC         Evidence={ECO:0000269|PubMed:16517619};
CC   -!- PATHWAY: Xenobiotic degradation; nitrobenzene degradation.
CC       {ECO:0000305|PubMed:16517619}.
CC   -!- PATHWAY: Xenobiotic degradation; 4-chloronitrobenzene degradation.
CC       {ECO:0000305|PubMed:16517619}.
CC   -!- SIMILARITY: Belongs to the amidase family. {ECO:0000305}.
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DR   EMBL; EF079106; ABB13583.2; -; Genomic_DNA.
DR   RefSeq; WP_008328889.1; NC_016978.1.
DR   RefSeq; YP_001967690.1; NC_010935.1.
DR   RefSeq; YP_005352119.1; NC_016978.1.
DR   AlphaFoldDB; Q38M35; -.
DR   SMR; Q38M35; -.
DR   PATRIC; fig|688245.4.peg.44; -.
DR   UniPathway; UPA00923; -.
DR   UniPathway; UPA01033; -.
DR   GO; GO:0050540; F:2-aminomuconate deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1300.10; -; 1.
DR   InterPro; IPR000120; Amidase.
DR   InterPro; IPR023631; Amidase_dom.
DR   InterPro; IPR036928; AS_sf.
DR   PANTHER; PTHR11895; PTHR11895; 1.
DR   Pfam; PF01425; Amidase; 1.
DR   SUPFAM; SSF75304; SSF75304; 1.
PE   1: Evidence at protein level;
KW   Aromatic hydrocarbons catabolism; Hydrolase; Plasmid.
FT   CHAIN           1..462
FT                   /note="2-amino-5-chloromuconic acid deaminase"
FT                   /id="PRO_0000441896"
FT   ACT_SITE        79
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:B9LZ18"
FT   ACT_SITE        156
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250|UniProtKB:B9LZ18"
FT   ACT_SITE        180
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:B9LZ18"
SQ   SEQUENCE   462 AA;  48856 MW;  E916FB216A1CE9A0 CRC64;
     MNAAHLSLAE HAARLRRREL TAVALIDTCA QHHARMEPRL NAYKTWDGAR ARSAAAAVDT
     LLDQGQDLGP LMGLPVSVKD LYGVPGLPVF AGSDEALPEA WQAAGPLVAR LQRQLGIVVG
     KTHTVEFAFG GLGVNAHWGT PRNPWSPHEH RVPGGSSAGA GVSLVQGSAL LALGTDTAGS
     VRVPASMTGQ VGLKTTVGRW PVEGIVPLSS SLDTAGVLTR TVEDLAYAFA ALDTESQGLP
     APAPVRVQGL RVGVPTNHFW DDIDPSIAAA VEAAVQRLAQ AGAQVVRFPL PHCEEAFDIF
     RRGGLAASEL AAYLDQHFPH KVERLDPVVR DRVRWAEQVS SVEYLRRKAV LQRCGAGAAR
     LFDDVDVLLT PTVPASPPRL ADIGTVETYA PANMKAMRNT AISNLFGWCA LTMPVGLDAN
     RMPVGLQLMG PPRAEARLIG IALGIEALIG QGHALLGAPD LP