ID A0A0D3AAB4_BRAOL Unreviewed; 578 AA.
AC A0A0D3AAB4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN Name=106312668 {ECO:0000313|EnsemblPlants:Bo1g091840.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo1g091840.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo1g091840.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo1g091840.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
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 RefSeq; XP_013605729.1; XM_013750275.1.
DR AlphaFoldDB; A0A0D3AAB4; -.
DR STRING; 109376.A0A0D3AAB4; -.
DR EnsemblPlants; Bo1g091840.1; Bo1g091840.1; Bo1g091840.
DR GeneID; 106312668; -.
DR Gramene; Bo1g091840.1; Bo1g091840.1; Bo1g091840.
DR KEGG; boe:106312668; -.
DR eggNOG; KOG2501; Eukaryota.
DR HOGENOM; CLU_019626_1_0_1; -.
DR OMA; WSYRCDE; -.
DR OrthoDB; 1201562at2759; -.
DR Proteomes; UP000032141; Chromosome C1.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0009860; P:pollen tube growth; IEA:EnsemblPlants.
DR GO; GO:0010183; P:pollen tube guidance; IEA:EnsemblPlants.
DR GO; GO:0080092; P:regulation of pollen tube growth; IEA:EnsemblPlants.
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; IPR017937; Thioredoxin_CS.
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; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000032141}.
FT DOMAIN 16..172
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 325..485
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT COILED 222..249
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 578 AA; 65187 MW; D33A2CD156D6EE78 CRC64;
MAEIAKEVNG GDARDLHSLL SSPARDFLIR KNGEQVKIDS LKGKKIGLYF SAAWCGPCQR
FTPQLVEIYN ELSSKVGFEV VFVSGDEDED SFKDYFSKMP WLAVPFTDSE TRDRLDEVFK
VRGIPNLVMI DDEGKLVNEN GVGVIRSYGA DAYPFTPEKM KEIKEEEERA RREQTLKSVL
VTPSRDFVIT RDGNKVPVSE LEGKTIGLLF SVASYRQCKE FTSKLEEVYK KLKENNEDFE
IVLISLEDDE DAFKQDFDTN PWLALPFNDK SSSKLTRHFM LSTLPTLVIL GPDGKTRHSN
VAEAIDDYGV VAYPFTPEKF EELKAIEKAK LEAQTLESLL VSGDLNYVLG KDGAKVLVSE
LVGKNILLYF SAHWCPPCRA FTPKLVEVYK QIKEKDEAFE LIFISSDRDQ ESFDEYYSQM
PWLALPFGDP RKTSLARTFK VGGIPMLAAL GPTGKTVTKE ARDLVGAHGA DAYPFTVERV
KEIEAKYTEM AKEWPEKVKH ALHEEHELEL TRVPVYICDQ CDEEGQIWSY HCDECDFDLH
AKCALKEDAN INGDDAVKEG GGEPQDGWVC DGNVCTKS
//
