ID   A0A1Z8UPT9_9PROT        Unreviewed;       303 AA.
AC   A0A1Z8UPT9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:OUU48961.1};
GN   ORFNames=CBC12_08055 {ECO:0000313|EMBL:OUU48961.1};
OS   Candidatus Puniceispirillum sp. TMED52.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster;
OC   Puniceispirillum.
OX   NCBI_TaxID=1986639 {ECO:0000313|EMBL:OUU48961.1, ECO:0000313|Proteomes:UP000195809};
RN   [1] {ECO:0000313|EMBL:OUU48961.1, ECO:0000313|Proteomes:UP000195809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMED52 {ECO:0000313|EMBL:OUU48961.1};
RA   Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT   "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT   for marine microbiology.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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:OUU48961.1}.
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DR   EMBL; NHDF01000097; OUU48961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z8UPT9; -.
DR   Proteomes; UP000195809; Unassembled WGS sequence.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02956; ybbN; 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   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..122
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   303 AA;  32594 MW;  F171D387BA71AF4A CRC64;
     MVSLQETTVH SGGGASVDVS TDSFMSEVVE ASRQQPVIVD FWAPWCGPCK QLMPILEKLV
     NETAGKVKLA KVNIDENQAI AAQLRVQSVP TVYVFQDGQP VDGFVGAKPE SELRDMVQQL
     AAHAGGGESV DSYLEQAEAA FAEKDYGAAI GAFQAVLHLE ENNEKAVAGL LRCLIGLNDL
     ENAKEMLDNL PDTLASSDAV QDVAKRLEFA LKASEQAGEL SVLQQAVVSD PENMQKRYDL
     AIAQFGSGAS EDAISTLLEM IRKNRGWNDD AARLQLLEIF AALGATAPEV KEGRKQLSSL
     LFS
//