ISOH_RHOSX
ID ISOH_RHOSX Reviewed; 226 AA.
AC Q9RBP5;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase {ECO:0000305};
DE EC=1.1.1.398 {ECO:0000269|PubMed:10094686};
GN Name=isoH {ECO:0000303|PubMed:10715003};
GN ORFNames=SZ00_06094 {ECO:0000312|EMBL:KJF19167.1};
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 2-24, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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).
CC -!- FUNCTION: Involved in isoprene degradation (PubMed:10094686,
CC PubMed:10715003). Catalyzes the two-step NAD(+)-dependent oxidation of
CC 2-glutathionyl-2-methylbut-3-en-1-ol (HGMB) to 2-glutathionyl-2-
CC methylbut-3-enoate (GMBA) (PubMed:10094686).
CC {ECO:0000269|PubMed:10094686, ECO:0000269|PubMed:10715003}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-glutathionyl-2-methylbut-3-en-1-ol + H2O + 2 NAD(+) = 2-
CC glutathionyl-2-methylbut-3-enoate + 3 H(+) + 2 NADH;
CC Xref=Rhea:RHEA:12156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:131718,
CC ChEBI:CHEBI:131797; EC=1.1.1.398;
CC Evidence={ECO:0000269|PubMed:10094686};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-glutathionyl-2-methylbut-3-en-1-ol + NAD(+) = 2-
CC glutathionyl-2-methylbut-3-enal + H(+) + NADH; Xref=Rhea:RHEA:49604,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:131718, ChEBI:CHEBI:131798;
CC Evidence={ECO:0000269|PubMed:10094686};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-glutathionyl-2-methylbut-3-enal + H2O + NAD(+) = 2-
CC glutathionyl-2-methylbut-3-enoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:49608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:131797,
CC ChEBI:CHEBI:131798; Evidence={ECO:0000269|PubMed:10094686};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.07 mM for NAD(+) {ECO:0000269|PubMed:10094686};
CC KM=1.4 mM for 2-glutathionyl-2-methylbut-3-en-1-ol
CC {ECO:0000269|PubMed:10094686};
CC Vmax=18 umol/min/mg enzyme {ECO:0000269|PubMed:10094686};
CC pH dependence:
CC Optimum pH is 9.0-10. {ECO:0000269|PubMed:10094686};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AJ249207; CAB55822.1; -; Genomic_DNA.
DR EMBL; JYOP01000009; KJF19167.1; -; Genomic_DNA.
DR RefSeq; WP_045063294.1; NZ_CM003191.1.
DR AlphaFoldDB; Q9RBP5; -.
DR SMR; Q9RBP5; -.
DR EnsemblBacteria; KJF19167; KJF19167; SZ00_06094.
DR KEGG; ag:CAB55822; -.
DR PATRIC; fig|103808.5.peg.69; -.
DR BioCyc; MetaCyc:MON-19833; -.
DR Proteomes; UP000032323; Plasmid unnamed.
DR Proteomes; UP000032323; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR Pfam; PF00106; adh_short; 1.
DR PRINTS; PR00081; GDHRDH.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase; Plasmid;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10094686"
FT CHAIN 2..226
FT /note="1-hydroxy-2-glutathionyl-2-methyl-3-butene
FT dehydrogenase"
FT /id="PRO_0000449974"
FT CONFLICT 24
FT /note="R -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 226 AA; 24062 MW; DB9BE2EA8C5594A0 CRC64;
MSTVLVVGAD KGIAHSISRQ LHDRGEDVIA ACLFDGADLA AAGITVEPGV DVTSQESVEA
LAARLSEKGV KLDAVFHVAG VMWLDEVGSL DYDLIRRQIE INTLGPLRTI EAVRPLLNEG
AKVGIVTSRV GSLGDNTSGG MYSYRISKAA ANMVGLNFHH DLSKDGVSVL LLHPGMVATD
LTKDFPGEHS YITPEQAAAG LIKNIDNLTP ETSGRFQHSD GTFLQW
