ID I3Z7G4_BELBD Unreviewed; 370 AA.
AC I3Z7G4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Peroxiredoxin {ECO:0000313|EMBL:AFL85182.1};
GN OrderedLocusNames=Belba_2637 {ECO:0000313|EMBL:AFL85182.1};
OS Belliella baltica (strain DSM 15883 / CIP 108006 / LMG 21964 / BA134).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Belliella.
OX NCBI_TaxID=866536 {ECO:0000313|EMBL:AFL85182.1, ECO:0000313|Proteomes:UP000006050};
RN [1] {ECO:0000313|Proteomes:UP000006050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15883 / CIP 108006 / LMG 21964 / BA134
RC {ECO:0000313|Proteomes:UP000006050};
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Davenport K., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Tindall B., Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Belliella baltica DSM 15883.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003281; AFL85182.1; -; Genomic_DNA.
DR RefSeq; WP_014773135.1; NC_018010.1.
DR AlphaFoldDB; I3Z7G4; -.
DR STRING; 866536.Belba_2637; -.
DR KEGG; bbd:Belba_2637; -.
DR PATRIC; fig|866536.3.peg.2720; -.
DR eggNOG; COG0526; Bacteria.
DR HOGENOM; CLU_042529_1_0_10; -.
DR OrthoDB; 6399635at2; -.
DR Proteomes; UP000006050; 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; IPR025380; DUF4369.
DR InterPro; IPR036249; Thioredoxin-like_sf.
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 Pfam; PF14289; DUF4369; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000006050}.
FT DOMAIN 232..370
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT COILED 122..149
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 370 AA; 41829 MW; 4E268D78833646C0 CRC64;
MKILQKFFFI LSTAVLFSCG ESEQVFDGEV KVAGKIENFD SNKVVLVQFI DDRTDVIDTL
KLGSNGKFNY DLTIEAPGFY ELIIGDKKSV RLALYDQDVE INYDVNNEDS LVILGSKDSQ
QMIKVQELMD DYQNKINELN DSYYEAMTNK DQESIKEIQT KAMNLEGDHA VKVKQVIDEM
DGSFAALAAI GMLNPKNDFI YIDELVSKLN TKYPDTKMIT TLMAQLEDMR ALSIGQTAPE
IALPNPDGEL VKLSDLRGKY VLIDFWAAWC KPCREENPNV VRLYNLYNEK GFEVFGVSLD
RTKEAWVQAI ADDGLTWTQV SDLKYFNSEA AATYQINAIP ATYLLDPEGK IIAKDLRGPS
LESKLKELFD
//