ID J9DZ31_9PROT Unreviewed; 108 AA.
AC J9DZ31;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN ORFNames=IMCC14465_07450 {ECO:0000313|EMBL:EJW20949.1};
OS alpha proteobacterium IMCC14465.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; PS1 clade.
OX NCBI_TaxID=1220535 {ECO:0000313|EMBL:EJW20949.1, ECO:0000313|Proteomes:UP000004836};
RN [1] {ECO:0000313|EMBL:EJW20949.1, ECO:0000313|Proteomes:UP000004836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC14465 {ECO:0000313|EMBL:EJW20949.1,
RC ECO:0000313|Proteomes:UP000004836};
RX PubMed=23209213; DOI=10.1128/JB.01888-12;
RA Yang S.J., Kang I., Cho J.C.;
RT "Genome Sequence of Strain IMCC14465, Isolated from the East Sea, Belonging
RT to the PS1 Clade of Alphaproteobacteria.";
RL J. Bacteriol. 194:6952-6953(2012).
CC -!- SIMILARITY: Belongs to the thioredoxin family.
CC {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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:EJW20949.1}.
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DR EMBL; ALYF01000003; EJW20949.1; -; Genomic_DNA.
DR AlphaFoldDB; J9DZ31; -.
DR STRING; 1220535.IMCC14465_07450; -.
DR PATRIC; fig|1220535.3.peg.742; -.
DR eggNOG; COG3118; Bacteria.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000004836; Unassembled WGS sequence.
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 InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR01068; thioredoxin; 1.
DR PANTHER; PTHR45663; GEO12009P1; 1.
DR PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PIRSF; PIRSF000077; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-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 ECO:0000256|PIRSR:PIRSR000077-4};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|PIRSR:PIRSR000077-4};
KW Reference proteome {ECO:0000313|Proteomes:UP000004836};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..108
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 37
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 28
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 35
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 36
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 34..37
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 108 AA; 11759 MW; 70A63B0E30501BFA CRC64;
MSDNAIINAS DSDFEETVLN ADTPVLVDFW AEWCGPCKQI APALEEIAAE MGNIKIVKVN
IDENPKTPTN YGVRSIPTMM IFQDGQTTAT KVGAAPKSDL VSWIEETV
//
