LINB_SPHIB
ID LINB_SPHIB Reviewed; 296 AA.
AC A0A1L5BTC1; P51698;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=Haloalkane dehalogenase {ECO:0000255|HAMAP-Rule:MF_01231};
DE EC=3.8.1.5 {ECO:0000255|HAMAP-Rule:MF_01231};
DE AltName: Full=1,3,4,6-tetrachloro-1,4-cyclohexadiene halidohydrolase {ECO:0000250|UniProtKB:D4Z2G1};
DE Short=1,4-TCDN halidohydrolase {ECO:0000250|UniProtKB:D4Z2G1};
GN Name=linB {ECO:0000303|PubMed:12450824};
GN ORFNames=SIDU_17345 {ECO:0000312|EMBL:APL96138.1};
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, 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 hydrolytic cleavage of carbon-halogen bonds in
CC halogenated aliphatic compounds, leading to the formation of the
CC corresponding primary alcohols, halide ions and protons (By
CC similarity). Is involved in the degradation of the important
CC environmental pollutant gamma-hexachlorocyclohexane (gamma-HCH or
CC lindane) as it also catalyzes conversion of 1,3,4,6-tetrachloro-1,4-
CC cyclohexadiene (1,4-TCDN) to 2,5-dichloro-2,5-cyclohexadiene-1,4-diol
CC (2,5-DDOL) via the intermediate 2,4,5-trichloro-2,5-cyclohexadiene-1-ol
CC (2,4,5-DNOL) (By similarity) (PubMed:12450824).
CC {ECO:0000250|UniProtKB:D4Z2G1, ECO:0000255|HAMAP-Rule:MF_01231,
CC ECO:0000305|PubMed:12450824}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-haloalkane + H2O = a halide anion + a primary alcohol +
CC H(+); Xref=Rhea:RHEA:19081, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15734, ChEBI:CHEBI:16042, ChEBI:CHEBI:18060; EC=3.8.1.5;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01231};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R,6R)-1,3,4,6-tetrachlorocyclohexa-1,4-diene + 2 H2O = 2,5-
CC dichlorocyclohexa-2,5-dien-1,4-diol + 2 chloride + 2 H(+);
CC Xref=Rhea:RHEA:11944, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17996, ChEBI:CHEBI:18904, ChEBI:CHEBI:28975;
CC Evidence={ECO:0000250|UniProtKB:D4Z2G1};
CC -!- PATHWAY: Xenobiotic degradation; gamma-hexachlorocyclohexane
CC degradation. {ECO:0000305|PubMed:12450824}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01231}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:D4Z2G1}.
CC -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01231}.
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DR EMBL; AY150581; AAN64241.1; -; Genomic_DNA.
DR EMBL; CP013070; APL96138.1; -; Genomic_DNA.
DR RefSeq; WP_007682110.1; NZ_CP013070.1.
DR AlphaFoldDB; A0A1L5BTC1; -.
DR SMR; A0A1L5BTC1; -.
DR ESTHER; sphpi-linb; Haloalkane_dehalogenase-HLD2.
DR EnsemblBacteria; APL96138; APL96138; SIDU_17345.
DR KEGG; sinb:SIDU_17345; -.
DR OrthoDB; 1890883at2; -.
DR UniPathway; UPA00689; -.
DR Proteomes; UP000004550; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR HAMAP; MF_01231; Haloalk_dehal_type2; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR023594; Haloalkane_dehalogenase_2.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Detoxification; Hydrolase; Periplasm.
FT CHAIN 1..296
FT /note="Haloalkane dehalogenase"
FT /id="PRO_0000444940"
FT DOMAIN 31..155
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
FT ACT_SITE 272
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01231"
SQ SEQUENCE 296 AA; 33230 MW; B14249854546F602 CRC64;
MSLGAKPFGE KKFIEIKGRR MAYIDEGTGD PILFQHGNPT SSYLWRNIMP HCAGLGRLIA
CDLIGMGDSD KLDPSGPERY TYAEHRDYLD ALWEALDLGD RVVLVVHDWG SVLGFDWARR
HRERVQGIAY MEAVTMPLEW ADFPEQDRDL FQAFRSQAGE ELVLQDNVFV EQVLPGLILR
PLSEAEMAAY REPFLAAGEA RRPTLSWPRQ IPIAGTPADV VAIARDYAGW LSESPIPKLF
INAEPGHLTT GRIRDFCRTW PNQTEITVAG AHFIQEDSPD EIGAAIAAFV RRLRPA
