ID   A0A0B6WUJ9_9BACT        Unreviewed;       455 AA.
AC   A0A0B6WUJ9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Thiol-disulfide isomerase-like thioredoxin {ECO:0000313|EMBL:CDM64676.1};
DE   Flags: Precursor;
GN   ORFNames=PYK22_00671 {ECO:0000313|EMBL:CDM64676.1};
OS   Pyrinomonas methylaliphatogenes.
OC   Bacteria; Acidobacteriota; Blastocatellia; Blastocatellales;
OC   Pyrinomonadaceae; Pyrinomonas.
OX   NCBI_TaxID=454194 {ECO:0000313|EMBL:CDM64676.1, ECO:0000313|Proteomes:UP000031518};
RN   [1] {ECO:0000313|EMBL:CDM64676.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM64676.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Stott M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDM64676.1, ECO:0000313|Proteomes:UP000031518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K22 {ECO:0000313|EMBL:CDM64676.1,
RC   ECO:0000313|Proteomes:UP000031518};
RA   Lee K.C.Y., Power J.F., Dunfield P.F., Morgan X.C., Huttenhower C.,
RA   Stott M.B.;
RT   "Complete genome sequence of Pyrinomonas methylaliphatogenes type strain
RT   K22T.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CBXV010000002; CDM64676.1; -; Genomic_DNA.
DR   RefSeq; WP_060635288.1; NZ_CBXV010000002.1.
DR   AlphaFoldDB; A0A0B6WUJ9; -.
DR   STRING; 454194.PYK22_00671; -.
DR   OrthoDB; 9811352at2; -.
DR   Proteomes; UP000031518; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Isomerase {ECO:0000313|EMBL:CDM64676.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031518};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..455
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002110283"
FT   DOMAIN          289..442
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   COILED          146..173
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   455 AA;  51793 MW;  EB2969409BF84541 CRC64;
     MVVKIALALA ISLLLDGAIS AQELPAPQRS EQETNAPKLP SARELYEEAA RYATRRFEEF
     DKKKLAFDRK LYEKTLQEQR ELAQTRAAQL SMRPNLAGED LYYLGLLFDL AGQAEGSLDA
     LRRFLREASN APGEMKQTAR VIIAIHAAQL KELKEAEQML AEYQRNEPRK AQEIFALERT
     LTSACYQAKD EDCALRHARA AFETAKQSYA ALDPAQRDRF LLAAADDLSI IYALHNQRDE
     LLGVLRELQR LGLKLPSAEL FRQATRRLRN YDGAEAEDLS NPERAIQQNE ESAPAPEIQA
     AEWIDTKPVR LADLRGRVVL LDFWAYWCGP CLEAFPKLRE WHQKYKDRGL TIIGLTRYYG
     AERGIPMAPK EELNFLREFK KRFKLPYGIG IEATEETALR YGVSSLPTSI LIDRRGMVRF
     ITVGINDEEL DKLGQWIEKL IAEPAPDEAR KAITQ
//