ID A0A0K9PYC2_ZOSMR Unreviewed; 429 AA.
AC A0A0K9PYC2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN ORFNames=ZOSMA_150G00150 {ECO:0000313|EMBL:KMZ73217.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ73217.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMZ73217.1}.
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DR EMBL; LFYR01000589; KMZ73217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9PYC2; -.
DR STRING; 29655.A0A0K9PYC2; -.
DR OMA; NAPCRQF; -.
DR OrthoDB; 1201562at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR CDD; cd03009; TryX_like_TryX_NRX; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
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:SF81; NUCLEOREDOXIN 3-RELATED; 1.
DR PANTHER; PTHR13871; THIOREDOXIN; 1.
DR Pfam; PF03107; C1_2; 1.
DR Pfam; PF13905; Thioredoxin_8; 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000036987}.
FT DOMAIN 170..335
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 429 AA; 49316 MW; 638F7017C8A58DD5 CRC64;
MMLLTLGNHF VKRCSQSSWL GIRFFWTPEK DMSMHCHHES FFAAESHDFL LTGNRKVPLS
SVDEKTTSVL FFFSSNWCRP CRKFTPLLID LYNSINNTTT KKLEIIFVSY DKDESTFTEY
HKLMPWLSAP FNSSLHKRLL HQYSIGRIPA LISSTSYGKA VGEDIVRLVE DYGVDAFPFS
AQRNEELKIM DFEKLQRGSL VDLLGSKTRD HVISKDGSKV LIASLIGKTI GLYFGANWCP
PCLSFTTILS QAYNEIHRLK KGEFEVIFVS TDRDEEEFKQ SIHDMPWLAI PYSENDRRDI
SRIFGVKGIP RLVILGSDGR TLEVDGRAMV CSYGAKAFPF TPTRVTELEM EIRKEGEELP
EHIMDYRHSH MLKLDRTKAY VCDLCKTRGK FWVFSCDECD FDVHPSCVQK NNIIVKCQAI
TRSPPLLHV
//
