ID   A0A0N9V547_SPHMC        Unreviewed;       541 AA.
AC   A0A0N9V547;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Thioredoxin domain-containing protein {ECO:0000259|PROSITE:PS51352};
GN   ORFNames=AN936_22405 {ECO:0000313|EMBL:ALH83006.1};
OS   Sphingopyxis macrogoltabida (Sphingomonas macrogoltabidus).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=33050 {ECO:0000313|EMBL:ALH83006.1, ECO:0000313|Proteomes:UP000058074};
RN   [1] {ECO:0000313|EMBL:ALH83006.1, ECO:0000313|Proteomes:UP000058074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EY-1 {ECO:0000313|EMBL:ALH83006.1,
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).
CC   -!- FUNCTION: May be required for disulfide bond formation in some
CC       proteins. {ECO:0000256|ARBA:ARBA00003565}.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. DsbA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005791}.
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DR   EMBL; CP012700; ALH83006.1; -; Genomic_DNA.
DR   RefSeq; WP_054589974.1; NZ_CP012700.1.
DR   AlphaFoldDB; A0A0N9V547; -.
DR   KEGG; smag:AN936_22405; -.
DR   PATRIC; fig|33050.5.peg.4635; -.
DR   OrthoDB; 9780147at2; -.
DR   Proteomes; UP000058074; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR041205; ScsC_N.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   Pfam; PF18312; ScsC_N; 1.
DR   Pfam; PF13462; Thioredoxin_4; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000058074};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        306..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          343..538
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          112..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   541 AA;  56253 MW;  24458D5931AB8C23 CRC64;
     MTDKKDDYYQ PWLRDPAPGA APHGAPPEPD AGLAKPKDVP PVGIDLTQYP ARERPAREAA
     TADHLKAGAA SLWQAIRTGA GAFADWTIRV GDRADIPARV EAMEIPRRSR ELAERSGRAA
     GRTARAIGKG SARAARATAD TGSQAWQKMA LGEKVAKISS DAGRGLGEVA GKTKAGIEQA
     AKAGSESLIG SIGEAATKLR PAPREEPAPP PSGLEQLLAR EEAAARAAEP AAPAAPDLPL
     FASEPALAPA PAPAKDVKSA AAAPDADDRT PHVRPAAKPA ASKAMAASKL PQVRGTGMDG
     VSGRTGLVAL AGIVLLAFAF WLGGRFGGGL GKSEVETIVA DYIKANPQII PEALEAQRGR
     EVAKAVDAIR PALEKPYAGA WAGNANGDVT LVVFTDYACG FCRASVPDVD RLIREDKRLK
     VVFRELPIIA PQSRDAALMA LAAARQGKYD AFHHAMFASP SLDKAAIAAA AEKVGVVTDG
     SADATANEAL FQRELDSNLA IATQLQLNAT PTWVVGDQLF QGQVGYDALR QAIAKARKAK
     G
//