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Database: UniProt
Entry: A0A142X2H5_9PLAN
LinkDB: A0A142X2H5_9PLAN
Original site: A0A142X2H5_9PLAN 
ID   A0A142X2H5_9PLAN        Unreviewed;       108 AA.
AC   A0A142X2H5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN   Name=trxA_5 {ECO:0000313|EMBL:AMV20964.1};
GN   ORFNames=VT03_23885 {ECO:0000313|EMBL:AMV20964.1};
OS   Planctomyces sp. SH-PL14.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctomyces.
OX   NCBI_TaxID=1632864 {ECO:0000313|EMBL:AMV20964.1, ECO:0000313|Proteomes:UP000076318};
RN   [1] {ECO:0000313|EMBL:AMV20964.1, ECO:0000313|Proteomes:UP000076318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL14 {ECO:0000313|EMBL:AMV20964.1,
RC   ECO:0000313|Proteomes:UP000076318};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987, ECO:0000256|PIRNR:PIRNR000077}.
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DR   EMBL; CP011270; AMV20964.1; -; Genomic_DNA.
DR   RefSeq; WP_075095272.1; NZ_CP011270.1.
DR   AlphaFoldDB; A0A142X2H5; -.
DR   STRING; 1632864.VT03_23885; -.
DR   KEGG; pls:VT03_23885; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000076318; Chromosome.
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:UP000076318};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..108
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        33
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   ACT_SITE        36
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            27
FT                   /note="Deprotonates C-terminal active site Cys"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT   SITE            34
FT                   /note="Contributes to redox potential value"
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   DISULFID        33..36
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ   SEQUENCE   108 AA;  11663 MW;  C899510E5FA4642D CRC64;
     MVGNVLDVTD ATFSSEVLDS ATPVLVDFWA TWCGPCLMLA PTVDALATEF AGKVKVCKVD
     VDKNRQSAVN YKIDAIPALF VFKGGQVVDR MKGAASKDQL KSMLNKHL
//
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