ID A0A022Q5L4_ERYGU Unreviewed; 567 AA.
AC A0A022Q5L4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=MIMGU_mgv1a003730mg {ECO:0000313|EMBL:EYU22493.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU22493.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU22493.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) +
CC NADH; Xref=Rhea:RHEA:18749, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00000696};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-dithiol + NADP(+) = [protein]-disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:18753, Rhea:RHEA-COMP:10593, Rhea:RHEA-
CC COMP:10594, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.8;
CC Evidence={ECO:0000256|ARBA:ARBA00001346};
CC -!- SIMILARITY: Belongs to the nucleoredoxin family.
CC {ECO:0000256|ARBA:ARBA00025782}.
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DR EMBL; KI632201; EYU22493.1; -; Genomic_DNA.
DR RefSeq; XP_012855292.1; XM_012999838.1.
DR AlphaFoldDB; A0A022Q5L4; -.
DR STRING; 4155.A0A022Q5L4; -.
DR GeneID; 105974703; -.
DR KEGG; egt:105974703; -.
DR eggNOG; KOG2501; Eukaryota.
DR OMA; WSYRCDE; -.
DR OrthoDB; 1201562at2759; -.
DR PhylomeDB; A0A022Q5L4; -.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR CDD; cd03009; TryX_like_TryX_NRX; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR004146; DC1.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR InterPro; IPR045870; TryX_NRX_thioredoxin_dom.
DR PANTHER; PTHR13871:SF96; NUCLEOREDOXIN 1-RELATED; 1.
DR PANTHER; PTHR13871; THIOREDOXIN; 1.
DR Pfam; PF03107; C1_2; 1.
DR Pfam; PF13905; Thioredoxin_8; 3.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000030748}.
FT DOMAIN 16..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 330..492
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 567 AA; 63977 MW; 22043BB481B65089 CRC64;
MESELEIANG DATYDLSSIL SSPNRDYLVR NNGDQVKFDS FKGKVTGLYF SASWCGPCQR
FTPKLVEAYN ELAQSNNFEI VFISGDEDDE SFDAYFSKMP WLAIPFSDSD TREKLNELFG
VSGIPHLVIL NEDGKILTSE GVQVIVENGS DGYPFTSEQI EKLRKQEEEA KMNQSLKSLL
VTESRDYVIT SDGKKVPVAE LEGKTVGLYF VLASYYGCLD FNSKLIEVYN SLREGGESFE
IVMVPLDEDE ESFGEEFEKL PWLSLPINDK CCLKLVRYFE LGALPTVVII GPNGKTLQSN
VVEAIEEHGM KAYPFTPEKF IELEEIEKAK REAQTLESLL VNQDSDYVIG EAGVKVPVSD
LNGKDILLYF SAHWCRPCRA FLPTLTKAYE EINKNNKRLE VIFISSDRDQ KAFEDYFSEM
PWLALPFGDK RKESLSSWFK VDGIPTLVAL GPTGKTVSTD ARGLIMAHGA EAYPFTRERI
EEIEKAFEKI LAGWAPNLKC GAHGHELFLT KRKNFVCDGC SEDGSVWSYY CEKCDFDLHP
KCAFDEESKD KTAAQEWVCD GDKCYKE
//
