LIND_SPHJU
ID LIND_SPHJU Reviewed; 346 AA.
AC D4Z909; P95806;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=2,5-dichlorohydroquinone reductive dechlorinase {ECO:0000303|PubMed:9515900};
DE Short=2,5-DCHQ dechlorinase {ECO:0000303|PubMed:9515900};
DE EC=2.5.1.- {ECO:0000269|PubMed:9515900};
DE AltName: Full=Glutathione-dependent reductive dehalogenase {ECO:0000303|PubMed:9515900};
GN Name=linD {ECO:0000303|PubMed:9515900};
GN OrderedLocusNames=SJA_P1-01390 {ECO:0000312|EMBL:BAI99091.1};
OS Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26 /
OS NBRC 101211 / UT26S).
OG Plasmid pCHQ1 {ECO:0000312|EMBL:BAI99091.1,
OG ECO:0000312|Proteomes:UP000007753}.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=452662;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND INDUCTION.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=9515900; DOI=10.1128/jb.180.6.1354-1359.1998;
RA Miyauchi K., Suh S.-K., Nagata Y., Takagi M.;
RT "Cloning and sequencing of a 2,5-dichlorohydroquinone reductive
RT dehalogenase gene whose product is involved in degradation of gamma-
RT hexachlorocyclohexane by Sphingomonas paucimobilis.";
RL J. Bacteriol. 180:1354-1359(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=20817768; DOI=10.1128/jb.00961-10;
RA Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A., Fukui S.,
RA Fujita N., Tsuda M.;
RT "Complete genome sequence of the representative gamma-
RT hexachlorocyclohexane-degrading bacterium Sphingobium japonicum UT26.";
RL J. Bacteriol. 192:5852-5853(2010).
CC -!- FUNCTION: Catalyzes the degradation of 2,5-dichlorohydroquinone (2,5-
CC DCHQ) into hydroquinone (HQ) via chlorohydroquinone (CHQ). Is involved
CC in the degradation pathway that allows S.japonicum UT26 to grow on
CC gamma-hexachlorocyclohexane (gamma-HCH or lindane) as the sole source
CC of carbon and energy. However, the conversion of CHQ to HQ by LinD
CC seems not to be essential for this degradation pathway, because the
CC conversion rate of CHQ to HQ is much lower than that of 2,5-DCHQ to
CC CHQ. CHQ is more efficiently degraded by LinE in strain UT26.
CC {ECO:0000269|PubMed:9515900}.
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:0000269|PubMed:9515900};
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:0000269|PubMed:9515900};
CC -!- PATHWAY: Xenobiotic degradation; gamma-hexachlorocyclohexane
CC degradation. {ECO:0000305|PubMed:9515900}.
CC -!- INDUCTION: By 2,5-dichlorohydroquinone. {ECO:0000269|PubMed:9515900}.
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:0000305|PubMed:9515900}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; D89733; BAA14011.1; -; Genomic_DNA.
DR EMBL; AP010805; BAI99091.1; -; Genomic_DNA.
DR RefSeq; WP_013035740.1; NC_014007.1.
DR AlphaFoldDB; D4Z909; -.
DR SMR; D4Z909; -.
DR EnsemblBacteria; BAI99091; BAI99091; SJA_P1-01390.
DR KEGG; sjp:SJA_P1-01390; -.
DR HOGENOM; CLU_794411_0_0_5; -.
DR OMA; PRFELFH; -.
DR UniPathway; UPA00689; -.
DR Proteomes; UP000007753; Plasmid pCHQ1.
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 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Detoxification; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..346
FT /note="2,5-dichlorohydroquinone reductive dechlorinase"
FT /id="PRO_0000186043"
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"
SQ SEQUENCE 346 AA; 38416 MW; 3E9A19F5E8BD04C0 CRC64;
MSADTETLAR KVREEVIKPE QSTLISPDRQ SPSLLRREAT VEPRFELFHF VFSVCSQKVR
GTLMEKGVTF GSNELTILPP QNENYCPQYV 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
