CPLR_DESHA
ID CPLR_DESHA Reviewed; 327 AA.
AC Q8GFE2;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Chlorophenol reductase;
DE AltName: Full=Ortho-chlorophenol reductive dehalogenase;
DE Flags: Precursor;
OS Desulfitobacterium hafniense (Desulfitobacterium frappieri).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=49338;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-39 AND 116-124,
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INDUCTION,
RP AND MASS SPECTROMETRY.
RC STRAIN=PCP-1 {ECO:0000269|PubMed:12697029};
RX PubMed=12697029; DOI=10.1042/bj20021837;
RA Boyer A., Page-Belanger R., Saucier M., Villemur R., Lepine F., Juteau P.,
RA Beaudet R.;
RT "Purification, cloning and sequencing of an enzyme mediating the reductive
RT dechlorination of 2,4,6-trichlorophenol from Desulfitobacterium frappieri
RT PCP-1.";
RL Biochem. J. 373:297-303(2003).
CC -!- FUNCTION: Reductive dechlorination of ortho-chlorophenols.
CC Dechlorinates in the ortho position with respect to the hydroxyl group.
CC {ECO:0000269|PubMed:12697029}.
CC -!- COFACTOR:
CC Name=cob(I)alamin; Xref=ChEBI:CHEBI:60488;
CC Evidence={ECO:0000269|PubMed:12697029};
CC -!- ACTIVITY REGULATION: Inhibited by sulfide and to a lesser extent by
CC nitrite. {ECO:0000269|PubMed:12697029}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12697029}. Secreted,
CC cell wall {ECO:0000269|PubMed:12697029}. Cell membrane
CC {ECO:0000269|PubMed:12697029}. Note=Associated with the cell membrane.
CC Probably binds to peptidoglycans of the cell membrane and cell wall.
CC -!- INDUCTION: By 2,4,6-trichlorophenol. {ECO:0000269|PubMed:12697029}.
CC -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC binding. {ECO:0000303|PubMed:12697029}.
CC -!- MASS SPECTROMETRY: Mass=33800; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12697029};
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DR EMBL; AY043467; AAK95329.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GFE2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009275; C:Gram-positive-bacterium-type cell wall; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0050781; F:ortho-trichlorophenol reductive dehalogenase activity; IDA:UniProtKB.
DR GO; GO:0046193; P:anaerobic phenol-containing compound catabolic process; IDA:UniProtKB.
DR CDD; cd00118; LysM; 1.
DR Gene3D; 3.10.350.10; -; 1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; SSF54106; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Cell membrane; Cell wall; Cobalamin;
KW Cobalt; Direct protein sequencing; Membrane; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:12697029"
FT CHAIN 25..327
FT /note="Chlorophenol reductase"
FT /id="PRO_0000020988"
FT DOMAIN 65..110
FT /note="LysM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
SQ SEQUENCE 327 AA; 35456 MW; 35B0EB9AE34BFECC CRC64;
MKKTLGIILS ISLAFSVLAL PIFAAVDTTT SATVEAATPA APATPAATAP AAAPSVDTSK
IAAGTYYTVV SGDFFWQIAA KHGLTIDALA KLNPQIKNVN LIFPGQKILV KAEEAAAAST
STSTAAVAPA AKKLYQGIGM AANYRDNTAR QKDHDNLNIT TVAALFDDAG KIVKLQFDVV
EILPDMFPGW MDPEAADKSF YKDAQANGFN WETKKEEGDA YGMKASAVSG KEWWEQMNFY
EEYFKGKTVA EVQDWFAKYC DANGRPYKMA YPEKLTDADK AKVATFTEAE KKMLVDVTTG
ATMSLQDPHS RFIDALVKAY EVRKEVK
