ID W1Q5K2_ABIDE Unreviewed; 103 AA.
AC W1Q5K2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Thioredoxin {ECO:0000256|ARBA:ARBA00020570, ECO:0000256|PIRNR:PIRNR000077};
GN ORFNames=GCWU000182_001280 {ECO:0000313|EMBL:ESK65119.1};
OS Abiotrophia defectiva ATCC 49176.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK65119.1, ECO:0000313|Proteomes:UP000019050};
RN [1] {ECO:0000313|EMBL:ESK65119.1, ECO:0000313|Proteomes:UP000019050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK65119.1,
RC ECO:0000313|Proteomes:UP000019050};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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:ESK65119.1}.
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DR EMBL; ACIN03000013; ESK65119.1; -; Genomic_DNA.
DR RefSeq; WP_023391922.1; NZ_KI535340.1.
DR AlphaFoldDB; W1Q5K2; -.
DR STRING; 592010.GCWU000182_001280; -.
DR GeneID; 84817787; -.
DR eggNOG; COG3118; Bacteria.
DR HOGENOM; CLU_090389_10_2_9; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000019050; 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:UP000019050};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..103
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 28
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 22
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 29
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 30
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT DISULFID 28..31
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 103 AA; 11549 MW; 54C33D3D99A7BDD6 CRC64;
MAKHLTDAEF LTSTAEGVTV VDFWAPWCGP CRMQGPVIDA LSEKYDGQVE FFKMNVDEEQ
KVAQEFGIMS IPTLLVKKDG QPVEKLIGYH DQAKLEAILA QYL
//
