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Identification
HMDB Protein ID HMDBP00826
Secondary Accession Numbers
  • 6107
  • HMDBP09355
Name Glutathione S-transferase A3
Synonyms
  1. GST class-alpha member 3
  2. Glutathione S-transferase A3-3
Gene Name GSTA3
Protein Type Enzyme
Biological Properties
General Function Involved in glutathione transferase activity
Specific Function Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Catalyzes isomerization reactions that contribute to the biosynthesis of steroid hormones. Efficiently catalyze obligatory double-bond isomerizations of delta(5)-androstene-3,17-dione and delta(5)-pregnene-3,20-dione, precursors to testosterone and progesterone, respectively.
Pathways
  • Chemical carcinogenesis
  • Drug metabolism - cytochrome P450
  • Glutathione metabolism
  • Metabolism of xenobiotics by cytochrome P450
Reactions
RX + Glutathione → HX + R-S-glutathione 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
glutathione metabolic process
xenobiotic metabolic process
Cellular Component
cytosol
Function
catalytic activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
glutathione transferase activity
Molecular Function
glutathione transferase activity
Process
metabolic process
physiological process
metabolism
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 6
Locus 6p12.1
SNPs GSTA3
Gene Sequence
>669 bp
ATGGCAGGGAAGCCCAAGCTTCACTACTTCAATGGACGGGGCAGAATGGAGCCCATCCGG
TGGCTCTTGGCTGCAGCTGGAGTGGAGTTTGAAGAGAAATTTATAGGATCTGCAGAAGAT
TTGGGAAAGTTAAGAAATGATGGGAGTTTGATGTTCCAGCAAGTACCAATGGTTGAGATT
GATGGGATGAAGTTGGTACAGACCAGAGCCATTCTCAACTACATTGCCAGCAAATACAAC
CTCTACGGGAAAGACATAAAGGAGAGAGCCCTAATTGATATGTATACAGAAGGTATGGCA
GATTTGAATGAAATGATCCTTCTTCTGCCCTTATGTCGACCTGAGGAAAAAGATGCCAAG
ATTGCCTTGATCAAAGAGAAAACAAAAAGTCGCTATTTCCCTGCCTTCGAAAAAGTGTTA
CAGAGCCATGGACAAGACTACCTTGTTGGCAACAAGCTGAGCCGGGCTGACATTAGCCTG
GTGGAACTTCTCTACTATGTGGAAGAGCTTGACTCCAGCCTTATCTCCAACTTCCCTCTG
CTGAAGGCCCTGAAAACCAGAATCAGCAACCTGCCCACGGTGAAGAAGTTTCTACAGCCT
GGCAGCCCAAGGAAGCCTCCCGCAGATGCAAAAGCTTTAGAAGAAGCCAGAAAGATTTTC
AGGTTTTAA
Protein Properties
Number of Residues 222
Molecular Weight 25301.355
Theoretical pI 9.196
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Glutathione S-transferase A3
MAGKPKLHYFNGRGRMEPIRWLLAAAGVEFEEKFIGSAEDLGKLRNDGSLMFQQVPMVEI
DGMKLVQTRAILNYIASKYNLYGKDIKERALIDMYTEGMADLNEMILLLPLCRPEEKDAK
IALIKEKTKSRYFPAFEKVLQSHGQDYLVGNKLSRADISLVELLYYVEELDSSLISNFPL
LKALKTRISNLPTVKKFLQPGSPRKPPADAKALEEARKIFRF
GenBank ID Protein 114731581
UniProtKB/Swiss-Prot ID Q16772
UniProtKB/Swiss-Prot Entry Name GSTA3_HUMAN
PDB IDs
GenBank Gene ID AF508266
GeneCard ID GSTA3
GenAtlas ID GSTA3
HGNC ID HGNC:4628
References
General References
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  2. 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 ]
  3. Suzuki T, Johnston PN, Board PG: Structure and organization of the human alpha class glutathione S-transferase genes and related pseudogenes. Genomics. 1993 Dec;18(3):680-6. [PubMed:8307579 ]
  4. Johansson AS, Mannervik B: Human glutathione transferase A3-3, a highly efficient catalyst of double-bond isomerization in the biosynthetic pathway of steroid hormones. J Biol Chem. 2001 Aug 31;276(35):33061-5. Epub 2001 Jun 20. [PubMed:11418619 ]
  5. Board PG: Identification of cDNAs encoding two human alpha class glutathione transferases (GSTA3 and GSTA4) and the heterologous expression of GSTA4-4. Biochem J. 1998 Mar 1;330 ( Pt 2):827-31. [PubMed:9480897 ]