LINE_SPHJU
ID LINE_SPHJU Reviewed; 321 AA.
AC Q9WXE6; D4Z913;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Chlorohydroquinone/hydroquinone 1,2-dioxygenase {ECO:0000305|PubMed:10542173};
DE EC=1.13.11.66 {ECO:0000269|PubMed:10542173};
DE AltName: Full=(Chloro)hydroquinone 1,2-dioxygenase {ECO:0000303|PubMed:10542173};
DE Short=(C)HQ 1,2-dioxygenase {ECO:0000303|PubMed:10542173};
GN Name=linE {ECO:0000303|PubMed:10542173};
GN OrderedLocusNames=SJA_P1-01430 {ECO:0000312|EMBL:BAI99095.1};
OS Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26 /
OS NBRC 101211 / UT26S).
OG Plasmid pCHQ1 {ECO:0000312|EMBL:BAI99095.1,
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, SUBSTRATE
RP SPECIFICITY, PATHWAY, INDUCTION, AND MUTAGENESIS OF HIS-162; HIS-229 AND
RP GLU-278.
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S;
RX PubMed=10542173; DOI=10.1128/jb.181.21.6712-6719.1999;
RA Miyauchi K., Adachi Y., Nagata Y., Takagi M.;
RT "Cloning and sequencing of a novel meta-cleavage dioxygenase gene whose
RT product is involved in degradation of gamma-hexachlorocyclohexane in
RT Sphingomonas paucimobilis.";
RL J. Bacteriol. 181:6712-6719(1999).
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: Cleaves aromatic rings with two hydroxyl groups at para
CC positions with consumption of O(2). Catalyzes the cleavage of
CC chlorohydroquinone (CHQ), as part of the gamma-hexachlorocyclohexane
CC (gamma-HCH or lindane) degradation pathway, producing 5-chlorocarbonyl-
CC 4-hydroxy-penta-2,4-dienoate as an intermediate product that can react
CC with water yielding maleylacetate. This degradation pathway allows
CC S.japonicum UT26 to grow on gamma-HCH as the sole source of carbon and
CC energy. Can also use hydroquinone (HQ) as substrate, leading to gamma-
CC hydroxymuconic semialdehyde. Is not able to convert catechol, contrary
CC to meta-cleavage dioxygenases. {ECO:0000269|PubMed:10542173}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydroquinone + O2 = (2E,4Z)-4-hydroxy-6-oxohexa-2,4-dienoate +
CC H(+); Xref=Rhea:RHEA:34163, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17594, ChEBI:CHEBI:66947; EC=1.13.11.66;
CC Evidence={ECO:0000269|PubMed:10542173};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorohydroquinone + O2 = 5-chlorocarbonyl-4-hydroxy-penta-
CC 2,4-dienoate + H(+); Xref=Rhea:RHEA:16761, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27675, ChEBI:CHEBI:140625;
CC Evidence={ECO:0000269|PubMed:10542173};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:10542173};
CC Note=Binds 1 Fe(2+) ion. {ECO:0000305|PubMed:10542173};
CC -!- PATHWAY: Xenobiotic degradation; gamma-hexachlorocyclohexane
CC degradation. {ECO:0000305|PubMed:10542173}.
CC -!- INDUCTION: By chlorohydroquinone, hydroquinone, and 2,5-
CC dichlorohydroquinone. {ECO:0000269|PubMed:10542173}.
CC -!- SIMILARITY: Belongs to the extradiol ring-cleavage dioxygenase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB021867; BAA76672.1; -; Genomic_DNA.
DR EMBL; AP010805; BAI99095.1; -; Genomic_DNA.
DR RefSeq; WP_007686007.1; NC_014007.1.
DR AlphaFoldDB; Q9WXE6; -.
DR SMR; Q9WXE6; -.
DR EnsemblBacteria; BAI99095; BAI99095; SJA_P1-01430.
DR KEGG; sjp:SJA_P1-01430; -.
DR HOGENOM; CLU_057821_0_0_5; -.
DR OMA; DHAIRGF; -.
DR BioCyc; MetaCyc:LINEPSEPA-MON; -.
DR BRENDA; 1.13.11.66; 2280.
DR UniPathway; UPA00689; -.
DR Proteomes; UP000007753; Plasmid pCHQ1.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.10.180.10; -; 2.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR037523; VOC.
DR Pfam; PF00903; Glyoxalase; 1.
DR SUPFAM; SSF54593; SSF54593; 1.
DR PROSITE; PS51819; VOC; 2.
PE 1: Evidence at protein level;
KW Aromatic hydrocarbons catabolism; Detoxification; Dioxygenase; Iron;
KW Metal-binding; Oxidoreductase; Plasmid; Reference proteome; Repeat.
FT CHAIN 1..321
FT /note="Chlorohydroquinone/hydroquinone 1,2-dioxygenase"
FT /id="PRO_0000085042"
FT DOMAIN 10..138
FT /note="VOC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT DOMAIN 160..282
FT /note="VOC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01163"
FT BINDING 162
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305|PubMed:10542173"
FT BINDING 229
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305|PubMed:10542173"
FT BINDING 278
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305|PubMed:10542173"
FT MUTAGEN 162
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:10542173"
FT MUTAGEN 229
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:10542173"
FT MUTAGEN 278
FT /note="E->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:10542173"
SQ SEQUENCE 321 AA; 35958 MW; 26ED662CB8B62826 CRC64;
MMQLPERVEG LHHITVATGS AQGDVDLLVK TLGQRLVKKT MFYDGARPVY HLYFGNELGE
PGTLYTTFPV RQAGYTGKRG AGQISAVSYN APVGTLSWWQ EHLIKRAVTV SEVRERFGQK
YLSFEHPDCG VGFEIIEQDT DGQFEPWDSP YVPKEVALRG FHSWTATLNR NEEMDSFMRN
AWNLKPQGRD GNYQRYAFGN GGAAKVLDVY IDEDERPGTW ALGEGQVHHA AFEVADLDVQ
AALKFDVEGL GYTDFSDRKH RGYFESIYVR TPGGVLFEAS VTLGFTHDES PEKLGSEVKV
APQLEGVKDE LLRTMNDPIV I
