ID   DCMA_METED              Reviewed;         288 AA.
AC   P21161; C7CG48;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   04-NOV-2026, entry version 124.
DE   RecName: Full=Dichloromethane dehalogenase;
DE            Short=DCM dehalogenase;
DE            EC=4.5.1.3;
GN   Name=dcmA; OrderedLocusNames=METDI2656;
OS   Methylorubrum extorquens (strain DSM 6343 / CIP 106787 / DM4)
OS   (Methylobacterium extorquens).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Methylobacteriaceae; Methylorubrum.
OX   NCBI_TaxID=661410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2104602; DOI=10.1128/jb.172.1.164-171.1990;
RA   la Roche S.D., Leisinger T.;
RT   "Sequence analysis and expression of the bacterial dichloromethane
RT   dehalogenase structural gene, a member of the glutathione S-transferase
RT   supergene family.";
RL   J. Bacteriol. 172:164-171(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6343 / CIP 106787 / DM4;
RX   PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA   Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA   Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA   Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA   Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA   Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA   Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA   Lidstrom M.E.;
RT   "Methylobacterium genome sequences: a reference blueprint to investigate
RT   microbial metabolism of C1 compounds from natural and industrial sources.";
RL   PLoS ONE 4:E5584-E5584(2009).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-15.
RA   Kohler-Staub D., Hartmans S., Gaelli R., Suter F., Leisinger T.;
RT   "Evidence for identical dichloromethane dehalogenases in different
RT   methylotrophic bacteria.";
RL   J. Gen. Microbiol. 132:2837-2843(1986).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dichloromethane + H2O = formaldehyde + 2 chloride + 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAX24312.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M32346; AAB68954.1; -; Genomic_DNA.
DR   EMBL; FP103042; CAX24312.1; ALT_INIT; Genomic_DNA.
DR   PIR; A47654; A47654.
DR   RefSeq; WP_041357702.1; NC_012988.1.
DR   AlphaFoldDB; P21161; -.
DR   SMR; P21161; -.
DR   GeneID; 72989601; -.
DR   KEGG; mdi:METDI2656; -.
DR   HOGENOM; CLU_965672_0_0_5; -.
DR   OMA; AANKMLP; -.
DR   BRENDA; 4.5.1.3; 3296.
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:0004364; F:glutathione transferase activity; IEA:TreeGrafter.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:TreeGrafter.
DR   CDD; cd03183; GST_C_Theta; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 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; IPR051369; GST_Theta.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43917; -; 1.
DR   PANTHER; PTHR43917:SF8; GH16740P-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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   CHAIN           1..288
FT                   /note="Dichloromethane dehalogenase"
FT                   /id="PRO_0000185990"
FT   DOMAIN          12..94
FT                   /note="GST N-terminal"
FT   DOMAIN          100..252
FT                   /note="GST C-terminal"
FT   VARIANT         1
FT                   /note="Missing (in 50 to 66% of the proteins)"
SQ   SEQUENCE   288 AA;  33112 MW;  3B79D2C3424FDF11 CRC64;
     MSPNPTNIHT GKTLRLLYHP ASQPCRSAHQ FMYEIDVPFE EEVVDISTDI TERQEFRDKY
     NPTGQVPILV DGEFTVWESV AIARYVNEKF DGAGNWFGRG TQERAQINQF LQWYAYTLRL
     GGGAFHWNIF GCLIYGEKPY SPKFTAEQNK GRTLLYEAMG TLENYWLRDR EYVCGDEVSY
     ADLAAFHEFV SHEAGKIIPD RVWQGFPKIA AWFKKLSERP HAKTVSEWQY TNVGKIIRGE
     LTASMFKRKT AVLKGTEVFS GHNHGIPYLN EKAEDYFKRV EKEGAAVA
//