ID G8P254_GRAMM Unreviewed; 208 AA.
AC G8P254;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:AEU38200.1};
DE Flags: Precursor;
GN OrderedLocusNames=AciX8_3917 {ECO:0000313|EMBL:AEU38200.1};
OS Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=682795 {ECO:0000313|EMBL:AEU38200.1, ECO:0000313|Proteomes:UP000007113};
RN [1] {ECO:0000313|EMBL:AEU38200.1, ECO:0000313|Proteomes:UP000007113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1857 / DSM 23137 / MP5ACTX8
RC {ECO:0000313|Proteomes:UP000007113};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Lu M., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Mikhailova N., Pagani I., Rawat S., Mannisto M.,
RA Haggblom M., Woyke T.;
RT "Complete sequence of Granulicella mallensis MP5ACTX8.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003130; AEU38200.1; -; Genomic_DNA.
DR RefSeq; WP_014267071.1; NC_016631.1.
DR AlphaFoldDB; G8P254; -.
DR STRING; 682795.AciX8_3917; -.
DR KEGG; gma:AciX8_3917; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_11_4_0; -.
DR Proteomes; UP000007113; Chromosome.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02966; TlpA_like_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR PANTHER; PTHR42852:SF6; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000007113}.
FT DOMAIN 62..204
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 43..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 208 AA; 22338 MW; F4C3A18BE7983BF6 CRC64;
MRRLGVLGAM VVVVALLVWA GVHNLRQRRL AMQQARQSQI TVVKDGATSS ASGDSPDAQG
ASLRGKPAPA FTLVDLSGKK VSLADYKGHA VVVNFWATWC GPCKLEMPWF EEFSGKYKSQ
GLVMLGLSQD QGASKDDIAD AAKKIGVTYQ ILLPDDNEKV SKAYGGVDYL PETFYVDKNG
NVVEETAGAP SKDEMEANIR KTLAVGGM
//
