ID C5WWQ2_SORBI Unreviewed; 584 AA.
AC C5WWQ2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=SORBI_3001G342600 {ECO:0000313|EMBL:EER94707.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER94707.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:EER94707.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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; CM000760; EER94707.1; -; Genomic_DNA.
DR RefSeq; XP_002467709.1; XM_002467664.1.
DR AlphaFoldDB; C5WWQ2; -.
DR STRING; 4558.C5WWQ2; -.
DR EnsemblPlants; EER94707; EER94707; SORBI_3001G342600.
DR GeneID; 8080431; -.
DR Gramene; EER94707; EER94707; SORBI_3001G342600.
DR KEGG; sbi:8080431; -.
DR eggNOG; KOG2501; Eukaryota.
DR HOGENOM; CLU_019626_1_0_1; -.
DR InParanoid; C5WWQ2; -.
DR OMA; WSYRCDE; -.
DR OrthoDB; 1201562at2759; -.
DR Proteomes; UP000000768; Chromosome 1.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR CDD; cd03009; TryX_like_TryX_NRX; 2.
DR Gene3D; 3.30.60.20; -; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT DOMAIN 3..170
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 333..493
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 584 AA; 64775 MW; B5C0E464B49EB3E2 CRC64;
MAEAEAEAAP AAAAGGGGIG DILATAERDF LVRNSGEQVK ISSIEASPVA IYFSASWCPP
CRRFTPKLIE VYKELAEQGK SFEVIFASAD QNEEGFNEYF AKMPWLAVPF SDTEGRAALD
ARFKVSGIPH LVILDAKTGE VYTEDGVEFV SEYGVEAYPF TPDRINELKE QEKAEKENQT
IQSVLGTSTR DYLISNKGDK VPISELEGKY VGLCFVVDGY GPVIEFTDSL AKIYEKLKEV
GEKFEVVAVS LDSEESAFNE SFAKMPWLAI PQGDQKCEKL VRYFELRSLP TLVLIGPDGK
TLNSNVADII DEHGFEAWEG FPFSAEKLEI LAEKAKAKAA SQTLESLLIS GDLDFVIGKG
GAKVPVSELV GKTVLLYFSA KWCGPCRAFL PTLVKEYNKI KEKNSDFEIV FISSDRDQSS
FDDFFSQMPW LALPLEDERK VSLKKTFKIR GIPSLVAIGP TGQTVSRDAK AQLMIHGADA
FPFTEERLEE LQKKLDEMAK GWPQKLKHEL HDEHELVLLR RGTYGCDGCE EMGSTWSYRC
DECDFDLHPK CALAEEKKGE EEEGKSTEEA PAGYVCEEGV CRKV
//
