Hmdb loader
Identification
HMDB Protein ID HMDBP00822
Secondary Accession Numbers
  • 6103
Name Glutathione S-transferase omega-1
Synonyms
  1. GSTO-1
  2. Glutathione S-transferase omega 1-1
  3. Glutathione-dependent dehydroascorbate reductase
  4. Monomethylarsonic acid reductase
  5. S-(Phenacyl)glutathione reductase
  6. GSTO 1-1
  7. MMA(V) reductase
  8. SPG-R
Gene Name GSTO1
Protein Type Enzyme
Biological Properties
General Function Involved in glutathione transferase activity
Specific Function Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid.
Pathways
  • Chemical carcinogenesis - DNA adducts
  • Drug metabolism - cytochrome P450
  • Glutathione metabolism
  • Metabolism of xenobiotics by cytochrome P450
Reactions
RX + Glutathione → HX + R-S-glutathione details
Glutathione + Dehydroascorbic acid → Oxidized glutathione + Ascorbic acid details
Methylarsonate + Glutathione → Methylarsonite + Oxidized glutathione + Water details
RX + Glutathione → Halide + R-S-Glutathione details
Naphthalene epoxide + Glutathione → (1R)-Hydroxy-(2R)-glutathionyl-1,2-dihydronaphthalene details
(1S,2R)-Naphthalene 1,2-oxide + Glutathione → (1R)-Glutathionyl-(2R)-hydroxy-1,2-dihydronaphthalene details
(1S,2R)-Naphthalene 1,2-oxide + Glutathione → (1S)-Hydroxy-(2S)-glutathionyl-1,2-dihydronaphthalene details
1-Nitronaphthalene-7,8-oxide + Glutathione → 1-Nitro-7-hydroxy-8-glutathionyl-7,8-dihydronaphthalene details
1-Nitronaphthalene-7,8-oxide + Glutathione → 1-Nitro-7-glutathionyl-8-hydroxy-7,8-dihydronaphthalene details
1-Nitronaphthalene-5,6-oxide + Glutathione → 1-Nitro-5-hydroxy-6-glutathionyl-5,6-dihydronaphthalene details
1-Nitronaphthalene-5,6-oxide + Glutathione → 1-Nitro-5-glutathionyl-6-hydroxy-5,6-dihydronaphthalene details
Bromobenzene-3,4-oxide + Glutathione → 3,4-Dihydro-3-hydroxy-4-S-glutathionyl bromobenzene details
Bromobenzene-2,3-oxide + Glutathione → 2,3-Dihydro-2-S-glutathionyl-3-hydroxy bromobenzene details
Benzo[a]pyrene-4,5-oxide + Glutathione → 4,5-Dihydro-4-hydroxy-5-S-glutathionyl-benzo[a]pyrene details
Benzo[a]pyrene-7,8-diol + Glutathione → 7,8-Dihydro-7-hydroxy-8-S-glutathionyl-benzo[a]pyrene + Water details
2,2-Dichloroacetaldehyde + Glutathione → S-(2,2-Dichloro-1-hydroxy)ethyl glutathione details
1,1-Dichloroethylene epoxide + Glutathione → 2-(S-Glutathionyl)acetyl chloride + Hydrochloric acid details
Chloroacetyl chloride + Glutathione → S-(2-Chloroacetyl)glutathione + Hydrochloric acid details
2-(S-Glutathionyl)acetyl chloride + Glutathione → 2-(S-Glutathionyl)acetyl glutathione + Hydrochloric acid details
Trichloroethylene + Glutathione → S-(1,2-Dichlorovinyl)glutathione + Hydrochloric acid details
1,2-Dibromoethane + Glutathione + Hydrogen Ion → Glutathione episulfonium ion + Bromide details
2-Bromoacetaldehyde + Glutathione → S-(Formylmethyl)glutathione + Bromide details
Aldophosphamide + Glutathione → 4-Glutathionyl cyclophosphamide + Water details
2,3-Epoxyaflatoxin B1 + Glutathione → Aflatoxin B1exo-8,9-epoxide-GSH details
GO Classification
Biological Process
cellular response to arsenic-containing substance
L-ascorbic acid metabolic process
regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
positive regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
negative regulation of ryanodine-sensitive calcium-release channel activity
positive regulation of ryanodine-sensitive calcium-release channel activity
L-ascorbic acid biosynthetic process
xenobiotic catabolic process
Cellular Component
cytosol
Component
cell part
intracellular part
cytoplasm
Function
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
glutathione transferase activity
Molecular Function
glutathione transferase activity
glutathione dehydrogenase (ascorbate) activity
methylarsonate reductase activity
Process
metabolic process
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 10
Locus 10q25.1
SNPs GSTO1
Gene Sequence
>726 bp
ATGTCCGGGGAGTCAGCCAGGAGCTTGGGGAAGGGAAGCGCGCCCCCGGGGCCGGTCCCG
GAGGGCTCGATCCGCATCTACAGCATGAGGTTCTGCCCGTTTGCTGAGAGGACGCGTCTA
GTCCTGAAGGCCAAGGGAATCAGGCATGAAGTCATCAATATCAACCTGAAAAATAAGCCT
GAGTGGTTCTTTAAGAAAAATCCCTTTGGTCTGGTGCCAGTTCTGGAAAACAGTCAGGGT
CAGCTGATCTACGAGTCTGCCATCACCTGTGAGTACCTGGATGAAGCATACCCAGGGAAG
AAGCTGTTGCCGGATGACCCCTATGAGAAAGCTTGCCAGAAGATGATCTTAGAGTTGTTT
TCTAAGGTGCCATCCTTGGTAGGAAGCTTTATTAGAAGCCAAAATAAAGAAGACTATGCT
GGCCTAAAAGAAGAATTTCGTAAAGAATTTACCAAGCTAGAGGAGGTTCTGACTAATAAG
AAGACGACCTTCTTTGGTGGCAATTCTATCTCTATGATTGATTACCTCATCTGGCCCTGG
TTTGAACGGCTGGAAGCAATGAAGTTAAATGAGTGTGTAGACCACACTCCAAAACTGAAA
CTGTGGATGGCAGCCATGAAGGAAGATCCCACAGTCTCAGCCCTGCTTACTAGTGAGAAA
GACTGGCAAGGTTTCCTAGAGCTCTACTTACAGAACAGCCCTGAGGCCTGTGACTATGGG
CTCTGA
Protein Properties
Number of Residues 241
Molecular Weight 27565.6
Theoretical pI 6.589
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Glutathione S-transferase omega-1
MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKP
EWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELF
SKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPW
FERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYG
L
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P78417
UniProtKB/Swiss-Prot Entry Name GSTO1_HUMAN
PDB IDs
GenBank Gene ID U90313
GeneCard ID GSTO1
GenAtlas ID GSTO1
HGNC ID HGNC:13312
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed:15164054 ]
  4. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  5. Hubbard MJ, McHugh NJ: Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis. 2000 Nov;21(17):3785-96. [PubMed:11271497 ]
  6. Board PG, Coggan M, Chelvanayagam G, Easteal S, Jermiin LS, Schulte GK, Danley DE, Hoth LR, Griffor MC, Kamath AV, Rosner MH, Chrunyk BA, Perregaux DE, Gabel CA, Geoghegan KF, Pandit J: Identification, characterization, and crystal structure of the Omega class glutathione transferases. J Biol Chem. 2000 Aug 11;275(32):24798-806. [PubMed:10783391 ]
  7. Yu L, Kalla K, Guthrie E, Vidrine A, Klimecki WT: Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans. Environ Health Perspect. 2003 Aug;111(11):1421-7. [PubMed:12928150 ]
  8. Whitbread AK, Tetlow N, Eyre HJ, Sutherland GR, Board PG: Characterization of the human Omega class glutathione transferase genes and associated polymorphisms. Pharmacogenetics. 2003 Mar;13(3):131-44. [PubMed:12618591 ]