ID K1PLR1_CRAGI Unreviewed; 309 AA.
AC K1PLR1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Thioredoxin reductase 2, mitochondrial {ECO:0000313|EMBL:EKC17395.1};
GN ORFNames=CGI_10000920 {ECO:0000313|EMBL:EKC17395.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC17395.1};
RN [1] {ECO:0000313|EMBL:EKC17395.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC17395.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532}.
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DR EMBL; JH822994; EKC17395.1; -; Genomic_DNA.
DR AlphaFoldDB; K1PLR1; -.
DR HOGENOM; CLU_016755_2_2_1; -.
DR InParanoid; K1PLR1; -.
DR OMA; HEENKEC; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR039648; DHPH_N.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF6; THIOREDOXIN REDUCTASE 2; 1.
DR Pfam; PF00070; Pyr_redox; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 56..222
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 239..288
FT /note="Pyridine nucleotide-disulphide oxidoreductase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF00070"
SQ SEQUENCE 309 AA; 33799 MW; 13B106FD10B7BE6E CRC64;
MNVPHQALKH AHLKVLDLNR DLVGAGSHRL GAGFLSAQSL LDGLQSPLDS SSTEDYDLVV
IGGGSGGLAC AKAASQLQKK VAVLDFVTPS TQGTTWGLGG TCVNVGCIPK KLMHHASLLG
DAIRDSKAYG WNVPDQVQSD WTTLSTAVQN HVKSLNWGHR VQLRDKNVEY INGLGSFKDP
HTVRVKESNG TERLLKTRNA VIAVGVRPYV PSQIPGAVEY GVTSDDLFWM KKSPGKTIMV
RSRPLKQFDQ QMAELVAESM ESKGTRFLRK CVPVSIEKDD RGRLVVKYED LTNRQTKEEV
FDTVMFATG
//
