ISOI_RHOSX
ID ISOI_RHOSX Reviewed; 238 AA.
AC Q9RBP4;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Isoprene-epoxide--glutathione S-transferase {ECO:0000305};
DE EC=4.4.1.34 {ECO:0000269|PubMed:10094686, ECO:0000269|PubMed:9687433};
GN Name=isoI {ECO:0000303|PubMed:10715003};
GN ORFNames=SZ00_06093 {ECO:0000312|EMBL:KJF19166.1};
OS Rhodococcus sp. (strain AD45).
OG Plasmid unnamed {ECO:0000312|Proteomes:UP000032323}.
OC Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX NCBI_TaxID=103808;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AD45;
RX PubMed=10715003; DOI=10.1128/jb.182.7.1956-1963.2000;
RA van Hylckama Vlieg J.E., Leemhuis H., Spelberg J.H., Janssen D.B.;
RT "Characterization of the gene cluster involved in isoprene metabolism in
RT Rhodococcus sp. strain AD45.";
RL J. Bacteriol. 182:1956-1963(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AD45; PLASMID=unnamed;
RX PubMed=25727256; DOI=10.1111/1462-2920.12793;
RA Crombie A.T., Khawand M.E., Rhodius V.A., Fengler K.A., Miller M.C.,
RA Whited G.M., McGenity T.J., Murrell J.C.;
RT "Regulation of plasmid-encoded isoprene metabolism in Rhodococcus, a
RT representative of an important link in the global isoprene cycle.";
RL Environ. Microbiol. 17:3314-3329(2015).
RN [3]
RP PROTEIN SEQUENCE OF 1-32, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=AD45;
RX PubMed=10094686; DOI=10.1128/jb.181.7.2094-2101.1999;
RA van Hylckama Vlieg J.E., Kingma J., Kruizinga W., Janssen D.B.;
RT "Purification of a glutathione S-transferase and a glutathione conjugate-
RT specific dehydrogenase involved in isoprene metabolism in Rhodococcus sp.
RT strain AD45.";
RL J. Bacteriol. 181:2094-2101(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC STRAIN=AD45;
RX PubMed=9687433; DOI=10.1128/aem.64.8.2800-2805.1998;
RA van Hylckama Vlieg J.E., Kingma J., van den Wijngaard A.J., Janssen D.B.;
RT "A glutathione S-transferase with activity towards cis-1,2-
RT dichloroepoxyethane is involved in isoprene utilization by Rhodococcus sp.
RT strain AD45.";
RL Appl. Environ. Microbiol. 64:2800-2805(1998).
CC -!- FUNCTION: Involved in isoprene degradation (PubMed:9687433,
CC PubMed:10094686, PubMed:10715003). Catalyzes the glutathione-dependent
CC ring opening of various epoxides (PubMed:9687433, PubMed:10094686). The
CC highest conversion rate is observed with the physiological substrate,
CC 3,4-epoxy-3-methyl-1-butene, which is the primary oxidation product of
CC isoprene (PubMed:9687433, PubMed:10094686). It can also use other
CC epoxides, including epoxyethane, epoxypropane, epithiopropane,
CC epichlorohydrin, epifluorohydrin, epibromohydrin, 1,2-epoxybutane, 1,2-
CC epoxyhexane, cis-2,3-epoxybutane, cis-1,2-dichloroepoxyethane and
CC trans-1,2-dichloroepoxyethane (PubMed:9687433, PubMed:10094686).
CC {ECO:0000269|PubMed:10094686, ECO:0000269|PubMed:10715003,
CC ECO:0000269|PubMed:9687433}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-glutathionyl-2-methylbut-3-en-1-ol = (3R)-3,4-epoxy-3-
CC methylbut-1-ene + glutathione; Xref=Rhea:RHEA:49568,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:131718, ChEBI:CHEBI:131720;
CC EC=4.4.1.34; Evidence={ECO:0000269|PubMed:10094686,
CC ECO:0000269|PubMed:9687433};
CC -!- ACTIVITY REGULATION: Activity is inhibited by 1,2-epoxyhexane.
CC {ECO:0000269|PubMed:9687433}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for 3,4-epoxy-3-methylbut-1-ene
CC {ECO:0000269|PubMed:10094686};
CC KM=0.1 mM for cis-1,2-dichloroepoxyethane
CC {ECO:0000269|PubMed:10094686};
CC Vmax=66 umol/min/mg enzyme with 3,4-epoxy-3-methylbut-1-ene as
CC substrate {ECO:0000269|PubMed:10094686};
CC Vmax=2.4 umol/min/mg enzyme with cis-1,2-dichloroepoxyethane as
CC substrate {ECO:0000269|PubMed:10094686};
CC pH dependence:
CC Optimum pH is 8.5-9.0. {ECO:0000269|PubMed:10094686};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10094686}.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; AJ249207; CAB55823.1; -; Genomic_DNA.
DR EMBL; JYOP01000009; KJF19166.1; -; Genomic_DNA.
DR RefSeq; WP_045063292.1; NZ_CM003191.1.
DR AlphaFoldDB; Q9RBP4; -.
DR SMR; Q9RBP4; -.
DR EnsemblBacteria; KJF19166; KJF19166; SZ00_06093.
DR KEGG; ag:CAB55823; -.
DR PATRIC; fig|103808.5.peg.68; -.
DR BioCyc; MetaCyc:MON-19832; -.
DR BRENDA; 4.4.1.34; 5397.
DR Proteomes; UP000032323; Plasmid unnamed.
DR Proteomes; UP000032323; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR InterPro; IPR026928; FAX/IsoI-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR033468; Metaxin_GST.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF17171; GST_C_6; 1.
DR Pfam; PF17172; GST_N_4; 1.
DR SFLD; SFLDG01200; SUF1.1; 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 Direct protein sequencing; Lyase; Plasmid; Reference proteome.
FT CHAIN 1..238
FT /note="Isoprene-epoxide--glutathione S-transferase"
FT /id="PRO_0000449973"
FT DOMAIN 7..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684"
FT DOMAIN 118..238
FT /note="GST C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685"
FT CONFLICT 28
FT /note="S -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 238 AA; 27094 MW; E715D9C4F7772798 CRC64;
MITVYGYVPA WGIPDISPYV TKVVNYLSFT GIEFEYKTQD LATLDQDSPH GKLPYIVDSD
GTKVGDSNTI IEYLKNKFGD KLDADLSKQQ LAQALAFHRL IEEHLYWSGI IQARWQDDAG
WETYIPFIVQ GAEVTPEMRV GLDAFRARIL DGFNGQGMGR RSEEVVAEFF RADIDALSDF
LDDKPFILGD KVHSIDASLY STLRHIADQP QQWLGSGYVQ TKPNLVDYLE RIRKQYDI
