LINA2_SPHIB
ID LINA2_SPHIB Reviewed; 156 AA.
AC P59767; A0A1L5BQ79;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Hexachlorocyclohexane dehydrochlorinase 2 {ECO:0000303|PubMed:12450824};
DE Short=HCH dehydrochlorinase 2 {ECO:0000303|PubMed:12450824};
DE EC=4.5.1.- {ECO:0000305|PubMed:12450824};
GN Name=linA2 {ECO:0000303|PubMed:12450824};
GN ORFNames=SIDU_11350 {ECO:0000312|EMBL:APL95055.1};
OS Sphingobium indicum (strain DSM 16412 / CCM 7286 / MTCC 6364 / B90A).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=861109;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP 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 SEQUENCE REVISION TO N-TERMINUS.
RA Lal R., Kumari R., Subudhi S., Suar M., Dhingra G., Raina V., Dogra C.,
RA Lal S.;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 conversion of the important environmental
CC pollutant gamma-hexachlorocyclohexane (gamma-HCH or lindane) to
CC 1,3,4,6-tetrachloro-1,4-cyclohexadiene (1,4-TCDN) via gamma-
CC pentachlorocyclohexene (gamma-PCCH) (PubMed:12450824). Proceeds by two
CC successive 1,2-anti conformationally dependent dehydrochlorinations (By
CC similarity). Also shows activity with alpha- and delta-HCH, giving
CC alpha- and delta-PCCH respectively, but not with the beta isomer
CC (PubMed:12450824). {ECO:0000250|UniProtKB:P51697,
CC ECO:0000269|PubMed:12450824}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-hexachlorocyclohexane = (3R,4S,5S,6R)-
CC pentachlorocyclohexene + chloride + H(+); Xref=Rhea:RHEA:45480,
CC ChEBI:CHEBI:10576, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996,
CC ChEBI:CHEBI:32888; Evidence={ECO:0000250|UniProtKB:P51697,
CC ECO:0000305|PubMed:12450824};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R,4S,5S,6R)-pentachlorocyclohexene = (3R,6R)-1,3,4,6-
CC tetrachlorocyclohexa-1,4-diene + chloride + H(+);
CC Xref=Rhea:RHEA:12152, ChEBI:CHEBI:10576, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:18904;
CC Evidence={ECO:0000250|UniProtKB:P51697};
CC -!- PATHWAY: Xenobiotic degradation; hexachlorocyclohexane degradation.
CC {ECO:0000269|PubMed:12450824}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P51697}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P51697}.
CC -!- MISCELLANEOUS: Is not N-terminally processed during export, so it may
CC be secreted into the periplasmic space via a hitherto unknown
CC mechanism. {ECO:0000250|UniProtKB:P51697}.
CC -!- MISCELLANEOUS: Gamma-hexachlorocyclohexane (lindane) is an
CC organochlorine insecticide which has been used worldwide since the
CC 1940s. Because of its toxicity and long persistence in soil, most
CC countries have prohibited the use of gamma-HCH. However, many
CC contaminated sites still remain throughout the world. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HCH dehydrochlorinase family. {ECO:0000305}.
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DR EMBL; AY150580; AAN64240.2; -; Genomic_DNA.
DR EMBL; CP013070; APL95055.1; -; Genomic_DNA.
DR RefSeq; WP_013040172.1; NZ_CP013070.1.
DR AlphaFoldDB; P59767; -.
DR SMR; P59767; -.
DR EnsemblBacteria; APL95055; APL95055; SIDU_11350.
DR KEGG; sinb:SIDU_11350; -.
DR OrthoDB; 1736098at2; -.
DR BRENDA; 4.5.1.B1; 8831.
DR UniPathway; UPA00690; -.
DR Proteomes; UP000004550; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR037401; SnoaL-like.
DR Pfam; PF13577; SnoaL_4; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW Detoxification; Lyase; Periplasm.
FT CHAIN 1..156
FT /note="Hexachlorocyclohexane dehydrochlorinase 2"
FT /id="PRO_0000084435"
FT ACT_SITE 25
FT /evidence="ECO:0000250|UniProtKB:P51697"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P51697"
SQ SEQUENCE 156 AA; 17342 MW; 2D96AF282FE1BCA0 CRC64;
MSDLDRLASR AAIQDLYSDK LIAVDKRQEG RLASIWWDDA EWTIEGIGTY KGPEGALDLA
NNVLWPMFHE CIHYGTNLRL EFVSADKVNG IGDVLLLGNL VEGNQSILIA AVFTDEYERR
DGVWKFSKRN ACTNYFTPLA GIHFAPPGIH FAPSGA
