ID A0A2W2DI06_9ACTN Unreviewed; 107 AA.
AC A0A2W2DI06;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Thioredoxin {ECO:0000256|PIRNR:PIRNR000077};
GN Name=trxA {ECO:0000313|EMBL:PZG00410.1};
GN ORFNames=C1I93_02630 {ECO:0000313|EMBL:PZG00410.1}, Jiend_28550
GN {ECO:0000313|EMBL:BCJ59433.1};
OS Micromonospora endophytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=515350 {ECO:0000313|EMBL:PZG00410.1, ECO:0000313|Proteomes:UP000248627};
RN [1] {ECO:0000313|EMBL:PZG00410.1, ECO:0000313|Proteomes:UP000248627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45430 {ECO:0000313|EMBL:PZG00410.1,
RC ECO:0000313|Proteomes:UP000248627};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Jishengella endophytica.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BCJ59433.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 109090 {ECO:0000313|EMBL:BCJ59433.1};
RA Komaki H., Tamura T.;
RT "Whole genome shotgun sequence of Jishengella endophytica NBRC 109090.";
RL Submitted (AUG-2020) 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; AP023358; BCJ59433.1; -; Genomic_DNA.
DR EMBL; POTX01000009; PZG00410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W2DI06; -.
DR KEGG; meno:Jiend_28550; -.
DR OrthoDB; 9790390at2; -.
DR Proteomes; UP000248627; Unassembled WGS sequence.
DR Proteomes; UP000682317; 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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 1..107
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 26
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-1"
FT SITE 33
FT /note="Contributes to redox potential value"
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 DISULFID 32..35
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000077-4"
SQ SEQUENCE 107 AA; 11534 MW; 4C55DF0E4D591DEC CRC64;
MGTTKSVTDA SFAADVLKSD KPVLVDFWAE WCGPCRKVSP LLEEIAGEMG DQVSIVKLNI
DENPETARAY RVMSVPTLTV FKNGEPVQSI AGAKPKGELV KLIQSAL
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