LINX_SPHIB
ID LINX_SPHIB Reviewed; 250 AA.
AC A0A1L5BU05; P50198;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 2.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=2,5-dichloro-2,5-cyclohexadiene-1,4-diol dehydrogenase LinX {ECO:0000250|UniProtKB:D4Z260};
DE Short=2,5-DDOL dehydrogenase {ECO:0000250|UniProtKB:D4Z260};
DE EC=1.1.1.- {ECO:0000250|UniProtKB:D4Z260};
GN Name=linX {ECO:0000303|PubMed:12450824};
GN ORFNames=SIDU_11340 {ECO:0000312|EMBL:APL96346.1},
GN SIDU_17875 {ECO:0000312|EMBL:APL96546.1};
OS Sphingobium indicum (strain DSM 16412 / CCM 7286 / MTCC 6364 / B90A).
OG Plasmid pSRL1 {ECO:0000312|EMBL:APL96546.1}.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=861109;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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-dichloro-2,5-cyclohexadiene-
CC 1,4-diol (2,5-DDOL) into 2,5-dichlorohydroquinone (2,5-DCHQ) in vitro.
CC LinX appears not to be involved in gamma-hexachlorocyclohexane (gamma-
CC HCH) degradation pathway, in contrast to LinC which has the same
CC enzymatic activity. {ECO:0000250|UniProtKB:D4Z260}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,5-dichlorocyclohexa-2,5-dien-1,4-diol + NAD(+) = 2,5-
CC dichlorohydroquinone + H(+) + NADH; Xref=Rhea:RHEA:15741,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:27545, ChEBI:CHEBI:28975,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000250|UniProtKB:D4Z260};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=APL96346.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=APL96546.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY150579; AAN64237.1; -; Genomic_DNA.
DR EMBL; CP013070; APL96346.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP013071; APL96546.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_007682029.1; NZ_CP013071.1.
DR AlphaFoldDB; A0A1L5BU05; -.
DR SMR; A0A1L5BU05; -.
DR EnsemblBacteria; APL96346; APL96346; SIDU_11340.
DR EnsemblBacteria; APL96546; APL96546; SIDU_17875.
DR KEGG; sinb:SIDU_11340; -.
DR KEGG; sinb:SIDU_17875; -.
DR OrthoDB; 1356861at2; -.
DR Proteomes; UP000004550; Chromosome.
DR Proteomes; UP000004550; Plasmid pSRL1.
DR GO; GO:0018502; F:2,5-dichloro-2,5-cyclohexadiene-1,4-diol dehydrogenase activity; IEA:RHEA.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Plasmid.
FT CHAIN 1..250
FT /note="2,5-dichloro-2,5-cyclohexadiene-1,4-diol
FT dehydrogenase LinX"
FT /id="PRO_0000444943"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 9..34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 250 AA; 25520 MW; 0B4CB3A6E8F5C9DD CRC64;
MANRLAGKVA LITGGASGLG AAQAKRFAEE GAKVVIGDLN EEMAKGVVAE IRAAGGDALF
IRLDVTDAAS WNNAIAAAVE AFGGLTTLSN TAGIIHPGGF EEESIEGWNK MVAVNQTAIF
LGIKAAIPEL VKSGNGSIIN ISSLIGMFPT AGNASYCATK AAVRIMSKAA ALEFVDRGVR
VNTIVPGGMN TPITANVPPD VLKQQTSQIP MGKLGDPIDI ANGALFLASD EAKYITGVDL
PIDGGWSVGV