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Database: UniProt
Entry: A0A0N9V327_SPHMC
LinkDB: A0A0N9V327_SPHMC
Original site: A0A0N9V327_SPHMC 
ID   A0A0N9V327_SPHMC        Unreviewed;       303 AA.
AC   A0A0N9V327;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:ALH82309.1};
GN   ORFNames=AN936_18725 {ECO:0000313|EMBL:ALH82309.1};
OS   Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH82309.1, ECO:0000313|Proteomes:UP000058074};
RN   [1] {ECO:0000313|EMBL:ALH82309.1, ECO:0000313|Proteomes:UP000058074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EY-1 {ECO:0000313|EMBL:ALH82309.1,
RC   ECO:0000313|Proteomes:UP000058074};
RX   PubMed=26634754;
RA   Ohtsubo Y., Nagata Y., Numata M., Tsuchikane K., Hosoyama A., Yamazoe A.,
RA   Tsuda M., Fujita N., Kawai F.;
RT   "Complete Genome Sequence of Polypropylene Glycol- and Polyethylene Glycol-
RT   Degrading Sphingopyxis macrogoltabida Strain EY-1.";
RL   Genome Announc. 3:0-0(2015).
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DR   EMBL; CP012700; ALH82309.1; -; Genomic_DNA.
DR   RefSeq; WP_054589369.1; NZ_CP012700.1.
DR   AlphaFoldDB; A0A0N9V327; -.
DR   KEGG; smag:AN936_18725; -.
DR   PATRIC; fig|33050.5.peg.3887; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000058074; Chromosome.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:UniProt.
DR   CDD; cd02956; ybbN; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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   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   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058074}.
FT   DOMAIN          8..116
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   303 AA;  31730 MW;  27B574AEE620E79B CRC64;
     MATLGLNPQE KEAVEAFRRD VVEPSMTSLV ILDFWAEWCG PCKQLAPTLE KVAADYADKG
     VVLAKVDVDA NPFIAGQFQV QSIPTVYAIF QGQPVANLTN ARSESQLKAI LDQLLAQLPI
     ESAASARAVE IAPLIEMGEN ILVEGDGPRA ASIFAQILDM APDNAAAHGG MIRALLLAGD
     IDGAQAALDA VPAEIAADPA VAQAKSALAL AADAPDAGEL AGFEATVAAN PDDHQARFDL
     AAAQIGAGQR DAAADNLLHI VAADREWQDG AARAKLLSLF EAVGLEDPWV AAQRRRLSLI
     LFG
//
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