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 27-MAR-2024, entry version 99. 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; Blattellidae; OC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CDD; cd03192; GST_C_Sigma_like; 1. DR CDD; cd03039; GST_N_Sigma_like; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. 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 PANTHER; PTHR11571; GLUTATHIONE S-TRANSFERASE; 1. DR PANTHER; PTHR11571:SF268; GLUTATHIONE S-TRANSFERASE S1; 1. DR Pfam; PF14497; GST_C_3; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDG01205; AMPS.1; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 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 //