ID   DCMA_METLD              Reviewed;         267 AA.
AC   P43387;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Dichloromethane dehalogenase;
DE            Short=DCM dehalogenase;
DE            EC=4.5.1.3;
GN   Name=dcmA;
OS   Methylophilus leisingeri (strain DSM 6813 / VKM B-2013 / DM11).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Methylophilaceae; Methylophilus.
OX   NCBI_TaxID=45393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-31.
RX   PubMed=8206823; DOI=10.1128/jb.176.12.3466-3473.1994;
RA   Bader R., Leisinger T.;
RT   "Isolation and characterization of the Methylophilus sp. strain DM11 gene
RT   encoding dichloromethane dehalogenase/glutathione S-transferase.";
RL   J. Bacteriol. 176:3466-3473(1994).
RN   [2]
RP   PRELIMINARY PROTEIN SEQUENCE OF 2-23.
RX   PubMed=3142855; DOI=10.1128/jb.170.12.5698-5704.1988;
RA   Scholtz R., Wackett L.P., Egli C., Cook A.M., Leisinger T.;
RT   "Dichloromethane dehalogenase with improved catalytic activity isolated
RT   from a fast-growing dichloromethane-utilizing bacterium.";
RL   J. Bacteriol. 170:5698-5704(1988).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dichloromethane + H2O = 2 chloride + formaldehyde + 2 H(+);
CC         Xref=Rhea:RHEA:15397, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15767, ChEBI:CHEBI:16842, ChEBI:CHEBI:17996; EC=4.5.1.3;
CC   -!- PATHWAY: Xenobiotic degradation; dichloromethane degradation.
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By dichloromethane.
CC   -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR   EMBL; L26544; AAA25443.1; -; Genomic_DNA.
DR   AlphaFoldDB; P43387; -.
DR   SMR; P43387; -.
DR   BRENDA; 4.5.1.3; 3320.
DR   SABIO-RK; P43387; -.
DR   UniPathway; UPA00688; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0018834; F:dichloromethane dehalogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd03183; GST_C_Theta; 1.
DR   CDD; cd03050; GST_N_Theta; 1.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR040077; GST_C_Theta.
DR   InterPro; IPR040075; GST_N_Theta.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Lyase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8206823"
FT   CHAIN           2..267
FT                   /note="Dichloromethane dehalogenase"
FT                   /id="PRO_0000185989"
FT   DOMAIN          3..85
FT                   /note="GST N-terminal"
FT   DOMAIN          91..224
FT                   /note="GST C-terminal"
SQ   SEQUENCE   267 AA;  31167 MW;  BCFE1606136CACA1 CRC64;
     MSTKLRYLHH PASQPCRAVH QFMLENNIEF QEEIVDITTD INEQPEFRER YNPTGQVPIL
     VDGDFTIWES AAIVYYLSEK YDCSSSWWGS TLEERGHIQQ YMHWYAYTLR LGGGAFHWTI
     FAPMIYGYDK DFTVEVTKGR FLLYESFDIL EKYWLKDGDY LCGNTLSYPD LATCQDLVSH
     DAGRIIPTSM WDSHPKVKAW FARMMDREHA KTVSAWQYEN VRKYLDDGVK LNFQRKTAVL
     KGTEVYSGHN NGIIYNGDDD SFVTQHG