ID G8PS14_PSEUV Unreviewed; 178 AA.
AC G8PS14;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Alkyl hydroperoxide reductase/ Thiol specific antioxidant/ Mal allergen {ECO:0000313|EMBL:AEV38549.1};
GN OrderedLocusNames=PSE_4045 {ECO:0000313|EMBL:AEV38549.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV38549.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV38549.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV38549.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
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; CP003147; AEV38549.1; -; Genomic_DNA.
DR RefSeq; WP_008547673.1; NC_016642.1.
DR AlphaFoldDB; G8PS14; -.
DR STRING; 911045.PSE_4045; -.
DR KEGG; psf:PSE_4045; -.
DR eggNOG; COG1225; Bacteria.
DR HOGENOM; CLU_132019_0_0_5; -.
DR Proteomes; UP000005634; Chromosome.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02970; PRX_like2; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00578; AhpC-TSA; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
FT DOMAIN 2..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 178 AA; 19511 MW; EB90E7B1B8E890D1 CRC64;
MLIPRKPVPS LSANLVGGGT FDLSADASDF ATLVVFYRGL HCPICATYLK ELERLTPEFE
ERGVKTIALS TDTEDRAQTF SNAIKADKLR VGYGVTLTKA REWGLFISAG RGKTSIGIEE
PDLFAEPGLF FVKPDGTLYF GNVQTMPFAR PDFKPMLGAL DFCIKNDYPA RGEYTGAL
//