GenomeNet

Database: UniProt
Entry: F3NB05_9ACTN
LinkDB: F3NB05_9ACTN
Original site: F3NB05_9ACTN 
ID   F3NB05_9ACTN            Unreviewed;       167 AA.
AC   F3NB05;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Alkyl hydroperoxide reductase subunit C-like protein {ECO:0000313|EMBL:EGG49464.1};
GN   ORFNames=SGM_0539 {ECO:0000313|EMBL:EGG49464.1};
OS   Streptomyces griseoaurantiacus M045.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG49464.1, ECO:0000313|Proteomes:UP000003022};
RN   [1] {ECO:0000313|EMBL:EGG49464.1, ECO:0000313|Proteomes:UP000003022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M045 {ECO:0000313|EMBL:EGG49464.1,
RC   ECO:0000313|Proteomes:UP000003022};
RX   PubMed=21551298; DOI=10.1128/JB.05053-11;
RA   Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT   "Draft genome sequence of the marine bacterium Streptomyces
RT   griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT   with a pABA core component.";
RL   J. Bacteriol. 193:3417-3418(2011).
CC   -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC       hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC       respectively. Plays a role in cell protection against oxidative stress
CC       by detoxifying peroxides. {ECO:0000256|ARBA:ARBA00037420}.
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:EGG49464.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AEYX01000002; EGG49464.1; -; Genomic_DNA.
DR   AlphaFoldDB; F3NB05; -.
DR   STRING; 996637.SGM_0539; -.
DR   eggNOG; COG1225; Bacteria.
DR   Proteomes; UP000003022; Unassembled WGS sequence.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd03018; PRX_AhpE_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR   PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003022}.
FT   DOMAIN          18..167
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        61
FT                   /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT                   peroxidase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ   SEQUENCE   167 AA;  18548 MW;  E25BD6ACB9C95937 CRC64;
     MENTPNSPTK GRSDIMALQV GDKAPDFALQ DNHGATVRLS DFRGEKNVVL LFYPFAFTGV
     CTGELCALRD NLPKFVNEDT QLLAVSNDSI HTLRVFAEQE GFEYPLLSDF WPHGETSRAY
     GVFAEDKGCA VRGTFVIDKE GVVRWTVVNA LPDARDLDEY VKALDTL
//
DBGET integrated database retrieval system