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Database: UniProt
Entry: H0A6C4_9PROT
LinkDB: H0A6C4_9PROT
Original site: H0A6C4_9PROT 
ID   H0A6C4_9PROT            Unreviewed;       232 AA.
AC   H0A6C4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Glutathione S-transferase protein {ECO:0000313|EMBL:EHL97172.1};
GN   ORFNames=HMPREF9946_04379 {ECO:0000313|EMBL:EHL97172.1};
OS   Acetobacteraceae bacterium AT-5844.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHL97172.1, ECO:0000313|Proteomes:UP000003292};
RN   [1] {ECO:0000313|EMBL:EHL97172.1, ECO:0000313|Proteomes:UP000003292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC       {ECO:0000256|RuleBase:RU003494}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHL97172.1}.
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DR   EMBL; AGEZ01000178; EHL97172.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0A6C4; -.
DR   STRING; 1054213.HMPREF9946_04379; -.
DR   PATRIC; fig|1054213.3.peg.3985; -.
DR   eggNOG; COG0625; Bacteria.
DR   HOGENOM; CLU_011226_14_4_5; -.
DR   OrthoDB; 9803562at2; -.
DR   BioCyc; ABAC1054213:G1H32-4047-MONOMER; -.
DR   Proteomes; UP000003292; Unassembled WGS sequence.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   CDD; cd10291; GST_C_YfcG_like; 1.
DR   CDD; cd03048; GST_N_Ure2p_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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR44051; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR44051:SF8; GLUTATHIONE S-TRANSFERASE-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDG01151; Main.2:_Nu-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000003292};
KW   Transferase {ECO:0000313|EMBL:EHL97172.1}.
FT   DOMAIN          1..87
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          90..215
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   REGION          207..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..232
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   232 AA;  26615 MW;  64D70DE02766102D CRC64;
     MTIEVWSWPT PNGHKVHIAL EELELPYKVV PVNIGKGEQF RPEFLAITPN HRIPAIVDPE
     GPDGRRVELF ESGAILIYLA EKSGRLMPSD PVERYKALQW LMFQMGGVGP MFGQYNHFAA
     YAPEKIPYAT ERYGNEVKRL HNVLEKRLSQ SEYLAGKDYS IADIATFPWV RNPDRRDIDL
     AEYPAVKRWH DAIAARPAVQ RGVAVLSENQ RSGPMNDEER ELLFGKTQYQ RR
//
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