GenomeNet

Database: UniProt
Entry: Q6A5E8_CUTAK
LinkDB: Q6A5E8_CUTAK
Original site: Q6A5E8_CUTAK 
ID   Q6A5E8_CUTAK            Unreviewed;       350 AA.
AC   Q6A5E8;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=Thioredoxin reductase {ECO:0000256|RuleBase:RU003880};
DE            EC=1.8.1.9 {ECO:0000256|RuleBase:RU003880};
GN   OrderedLocusNames=PPA2309 {ECO:0000313|EMBL:AAT84015.1};
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Cutibacterium.
OX   NCBI_TaxID=267747 {ECO:0000313|EMBL:AAT84015.1, ECO:0000313|Proteomes:UP000000603};
RN   [1] {ECO:0000313|EMBL:AAT84015.1, ECO:0000313|Proteomes:UP000000603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202 {ECO:0000313|Proteomes:UP000000603};
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Bruggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Durre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC         H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000849,
CC         ECO:0000256|RuleBase:RU003880};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU003881};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003881};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003880}.
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003880}.
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; AE017283; AAT84015.1; -; Genomic_DNA.
DR   RefSeq; WP_002515813.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6A5E8; -.
DR   ChEMBL; CHEMBL2364151; -.
DR   EnsemblBacteria; AAT84015; AAT84015; PPA2309.
DR   GeneID; 66622196; -.
DR   KEGG; pac:PPA2309; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_1_11; -.
DR   OMA; FRAEDYW; -.
DR   Proteomes; UP000000603; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   NCBIfam; TIGR01292; TRX_reduct; 1.
DR   PANTHER; PTHR48105:SF16; THIOREDOXIN REDUCTASE 1-RELATED; 1.
DR   PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|RuleBase:RU003880};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003880};
KW   NADP {ECO:0000256|RuleBase:RU003881};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003880};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003880}.
FT   DOMAIN          45..334
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   350 AA;  37263 MW;  765EDE92173479F0 CRC64;
     MTTQALTPNT ILGNISLSDP SEIDTTQPFP ETVGADVHGN DEPRDVIIVG SGPAGYTAAV
     YTARAGLKPL VFEGSMDAGG ALMQTTEVEN YPGFSEGIMG PDLMAQMRAQ AERFGAELIA
     DDVTDIDLTG EIKKLVDTDG NTYKAHVVIL AMGSAYRKLG LEDEPRLSGR GVSWCATCDG
     FFFTGKDIAV VGGGDSAVEE ATFLTRFANS VTLVHRRDQL RASQIMADRA AADPKITFAW
     NSEVVAMQGE SKLESITLRD TKTGEERQLE VAGVFEAIGH DPRSELVRGQ VDLDDAGYVV
     CAEPSTRTNV PGVFACGDLV DSHYQQAVTA AGSGCRAALD AERFLTELGR
//
DBGET integrated database retrieval system