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GST1_BLAGE
ID   GST1_BLAGE              Reviewed;         204 AA.
AC   O18598;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-sigma;
DE   AltName: Full=Major allergen Bla g 5;
DE   AltName: Allergen=Bla g 5;
OS   Blattella germanica (German cockroach) (Blatta germanica).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blaberoidea; Ectobiidae;
OC   Blattellinae; Blattella.
OX   NCBI_TaxID=6973;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-204, AND PROTEIN SEQUENCE OF 2-39.
RX   PubMed=9252418; DOI=10.1074/jbc.272.33.20907;
RA   Arruda L.K., Vailes L.D., Platts-Mills T.A.E., Hayden M.L., Chapman M.D.;
RT   "Induction of IgE antibody responses by glutathione S-transferase from the
RT   German cockroach (Blattella germanica).";
RL   J. Biol. Chem. 272:20907-20912(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC   -!- ALLERGEN: Causes an allergic reaction in human. Causes positive
CC       immediate skin tests in cockroach-allergic patients using as little as
CC       3 pg of recombinant protein. Associated with asthma.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC       {ECO:0000305}.
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DR   EMBL; U92412; AAB72147.1; -; mRNA.
DR   PDB; 4Q5R; X-ray; 2.25 A; A/B/C/D/E/F=1-204.
DR   PDBsum; 4Q5R; -.
DR   AlphaFoldDB; O18598; -.
DR   SMR; O18598; -.
DR   Allergome; 144; Bla g 5.
DR   Allergome; 3142; Bla g 5.0101.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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   3D-structure; Allergen; Direct protein sequencing; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9252418"
FT   CHAIN           2..204
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185916"
FT   DOMAIN          3..80
FT                   /note="GST N-terminal"
FT   DOMAIN          82..204
FT                   /note="GST C-terminal"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         40
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         44
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P46088"
FT   BINDING         50..52
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         64..65
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   CONFLICT        10
FT                   /note="C -> F (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..9
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   STRAND          11..13
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           17..25
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   STRAND          31..34
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           65..75
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           83..107
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           112..124
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           126..140
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   STRAND          143..146
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           152..168
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   TURN            172..175
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           177..188
FT                   /evidence="ECO:0007829|PDB:4Q5R"
FT   HELIX           190..198
FT                   /evidence="ECO:0007829|PDB:4Q5R"
SQ   SEQUENCE   204 AA;  23334 MW;  4CBE9339C913551C CRC64;
     MAPSYKLTYC PVKALGEPIR FLLSYGEKDF EDYRFQEGDW PNLKPSMPFG KTPVLEIDGK
     QTHQSVAISR YLGKQFGLSG KDDWENLEID MIVDTISDFR AAIANYHYDA DENSKQKKWD
     PLKKETIPYY TKKFDEVVKA NGGYLAAGKL TWADFYFVAI LDYLNHMAKE DLVANQPNLK
     ALREKVLGLP AIKAWVAKRP PTDL
 
 
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