LIND_SPHIB
ID LIND_SPHIB Reviewed; 346 AA.
AC A0A1L5BUX8; P95806;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=2,5-dichlorohydroquinone reductive dechlorinase {ECO:0000250|UniProtKB:D4Z909};
DE Short=2,5-DCHQ dechlorinase {ECO:0000250|UniProtKB:D4Z909};
DE EC=2.5.1.- {ECO:0000250|UniProtKB:D4Z909};
DE AltName: Full=Glutathione-dependent reductive dehalogenase {ECO:0000250|UniProtKB:D4Z909};
GN Name=linD {ECO:0000303|PubMed:12450824};
GN ORFNames=SIDU_18555 {ECO:0000312|EMBL:APL96652.1};
OS Sphingobium indicum (strain DSM 16412 / CCM 7286 / MTCC 6364 / B90A).
OG Plasmid pSRL3 {ECO:0000312|Proteomes:UP000004550}.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=861109;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=B90;
RX PubMed=12450824; DOI=10.1128/aem.68.12.6021-6028.2002;
RA Kumari R., Subudhi S., Suar M., Dhingra G., Raina V., Dogra C., Lal S.,
RA van der Meer J.R., Holliger C., Lal R.;
RT "Cloning and characterization of lin genes responsible for the degradation
RT of hexachlorocyclohexane isomers by Sphingomonas paucimobilis strain B90.";
RL Appl. Environ. Microbiol. 68:6021-6028(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16412 / CCM 7286 / MTCC 6364 / B90A;
RX PubMed=22843598; DOI=10.1128/jb.00901-12;
RA Anand S., Sangwan N., Lata P., Kaur J., Dua A., Singh A.K., Verma M.,
RA Kaur J., Khurana J.P., Khurana P., Mathur S., Lal R.;
RT "Genome sequence of Sphingobium indicum B90A, a hexachlorocyclohexane-
RT degrading bacterium.";
RL J. Bacteriol. 194:4471-4472(2012).
CC -!- FUNCTION: Catalyzes the degradation of 2,5-dichlorohydroquinone (2,5-
CC DCHQ) into hydroquinone (HQ) via chlorohydroquinone (CHQ).
CC {ECO:0000250|UniProtKB:D4Z909, ECO:0000305|PubMed:12450824}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,5-dichlorohydroquinone + 2 glutathione = chloride +
CC chlorohydroquinone + glutathione disulfide + H(+);
CC Xref=Rhea:RHEA:53012, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:27545, ChEBI:CHEBI:27675, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297; Evidence={ECO:0000250|UniProtKB:D4Z909};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorohydroquinone + 2 glutathione = chloride + glutathione
CC disulfide + H(+) + hydroquinone; Xref=Rhea:RHEA:53016,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17594, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:27675, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297;
CC Evidence={ECO:0000250|UniProtKB:D4Z909};
CC -!- PATHWAY: Xenobiotic degradation; gamma-hexachlorocyclohexane
CC degradation. {ECO:0000305|PubMed:12450824}.
CC -!- MISCELLANEOUS: The mechanism of this reaction probably involves a
CC glutathione transfer: the halogen is firstly removed through
CC substitution with glutathione, which is then removed by displacement of
CC the aromatic moiety by a second glutathione molecule, producing
CC oxidized glutathione (GS-SG). {ECO:0000250|UniProtKB:D4Z909}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=APL96652.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY150583; AAN64243.1; -; Genomic_DNA.
DR EMBL; CP013073; APL96652.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_031293069.1; NZ_CP013073.1.
DR AlphaFoldDB; A0A1L5BUX8; -.
DR SMR; A0A1L5BUX8; -.
DR EnsemblBacteria; APL96652; APL96652; SIDU_18555.
DR KEGG; sinb:SIDU_18555; -.
DR OrthoDB; 1383885at2; -.
DR UniPathway; UPA00689; -.
DR Proteomes; UP000004550; Plasmid pSRL3.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF13409; GST_N_2; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; Detoxification; Plasmid; Transferase.
FT CHAIN 1..346
FT /note="2,5-dichlorohydroquinone reductive dechlorinase"
FT /id="PRO_0000444942"
FT DOMAIN 43..154
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 189..335
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT CONFLICT 206
FT /note="K -> R (in Ref. 1; AAN64243)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38389 MW; 3862D4F5E74E34C0 CRC64;
MSADTETLAR KVREEVIKPE QSTLISPDRQ SPSLLRREAT VEPRFELFHF VFSVCSQKVR
GTLMEKGVTF GSNELTILPP QSENYCPQYV RLRLRSEAAA KHRPVSSFTG QSSVDSEGFD
PLVVPTLVDH ETGRILADSK AICLYLCDAL SGGTDLLPAD IREAVLKQVQ LADTTPHVAL
LYGADPDGDR RPESMQAVMP GIHAHKIDAV RRNIPLADGD PLLLEAYQHK IVKEEAAASF
VINEPQMRTA ISKAEQLVTD LDRDLGASTG PWLFGDRFTL ADLFWAVSLY RFLWLGYSGF
WKDGAGKPRV EAYANRLFAR PSVKDAIIQW PGHPPSENVI HLLSNA
