ID A0A090AGM3_9GAMM Unreviewed; 287 AA.
AC A0A090AGM3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Thioredoxin {ECO:0000313|EMBL:BAP54362.1};
GN ORFNames=THII_0065 {ECO:0000313|EMBL:BAP54362.1};
OS Thioploca ingrica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Thioploca.
OX NCBI_TaxID=40754 {ECO:0000313|EMBL:BAP54362.1, ECO:0000313|Proteomes:UP000031623};
RN [1] {ECO:0000313|EMBL:BAP54362.1, ECO:0000313|Proteomes:UP000031623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kojima H., Ogura Y., Yamamoto N., Togashi T., Mori H., Watanabe T.,
RA Nemoto F., Kurokawa K., Hayashi T., Fukui M.;
RT "Ecophysiology of Thioploca ingrica as revealed by the complete genome
RT sequence supplemented with proteomic evidence.";
RL ISME J. 0:0-0(2014).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987}.
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DR EMBL; AP014633; BAP54362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090AGM3; -.
DR STRING; 40754.THII_0065; -.
DR KEGG; tig:THII_0065; -.
DR HOGENOM; CLU_046120_1_0_6; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000031623; Chromosome.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR Pfam; PF14559; TPR_19; 1.
DR Pfam; PF14561; TPR_20; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000031623};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 6..113
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 287 AA; 32340 MW; 914F4DDE26A10D3D CRC64;
MNHSPYIIII TAQNFTPEVI EKSRQVPVLV DFWAAWCAPC KMILPVLTKL ADEYQGKFIL
AKVNTDEEQQ LASQYSIRSI PTLKLFRHGQ VVEDIMGAQP ESVLRDMIDR HCERPADRLR
SQAMAAHLSG NTEQAIALLE QARNMEPSYY PVQLDLAKIL LEVKRFEEAQ QLLKNLPVNV
QMEPAVNELI AHLTFAAVAD KAPTALSLEQ AIAANPNDHQ ARYQLSAQQI LTGDYETAME
HLLELMHRDR GFEDDAGRKG LLAVFTLLGN QGSIVSRYRS KMSSLLY
//
