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Database: UniProt
Entry: A0A2I0VGA8_9ASPA
LinkDB: A0A2I0VGA8_9ASPA
Original site: A0A2I0VGA8_9ASPA 
ID   A0A2I0VGA8_9ASPA        Unreviewed;       604 AA.
AC   A0A2I0VGA8;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=protein-disulfide reductase {ECO:0000256|ARBA:ARBA00012612};
DE            EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
GN   ORFNames=MA16_Dca022537 {ECO:0000313|EMBL:PKU62449.1};
OS   Dendrobium catenatum.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Malaxideae; Dendrobiinae; Dendrobium.
OX   NCBI_TaxID=906689 {ECO:0000313|EMBL:PKU62449.1, ECO:0000313|Proteomes:UP000233837};
RN   [1] {ECO:0000313|EMBL:PKU62449.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU62449.1};
RX   PubMed=26754549; DOI=10.1038/srep19029;
RA   Zhang G.Q., Xu Q., Bian C., Tsai W.C., Yeh C.M., Liu K.W., Yoshida K.,
RA   Zhang L.S., Chang S.B., Chen F., Shi Y., Su Y.Y., Zhang Y.Q., Chen L.J.,
RA   Yin Y., Lin M., Huang H., Deng H., Wang Z.W., Zhu S.L., Zhao X., Deng C.,
RA   Niu S.C., Huang J., Wang M., Liu G.H., Yang H.J., Xiao X.J., Hsiao Y.Y.,
RA   Wu W.L., Chen Y.Y., Mitsuda N., Ohme-Takagi M., Luo Y.B., Van de Peer Y.,
RA   Liu Z.J.;
RT   "The Dendrobium catenatum Lindl. genome sequence provides insights into
RT   polysaccharide synthase, floral development and adaptive evolution.";
RL   Sci. Rep. 6:19029-19029(2016).
RN   [2] {ECO:0000313|EMBL:PKU62449.1, ECO:0000313|Proteomes:UP000233837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=The whole plant {ECO:0000313|EMBL:PKU62449.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(2017).
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; KZ503646; PKU62449.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I0VGA8; -.
DR   STRING; 906689.A0A2I0VGA8; -.
DR   Proteomes; UP000233837; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR13871; THIOREDOXIN; 1.
DR   PANTHER; PTHR13871:SF7; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 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; 2.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233837};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        99..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          205..366
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          370..528
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          65..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   604 AA;  66293 MW;  9126C46CB8FF6143 CRC64;
     MDKEDDETIS FAGMACHVSP SPETSRNPSP PGDPLFEFRP SPELSYPSSP ADLLFSNGLL
     LPRSLPPETG ANDRPRCLKD PAGHRGGSRK LTMSASKRVS FQLVITTTIL SIIALLWMQD
     RRRRSPEGQS NKLGTVDDMS GRWLDDQGGR KLGGGGRSAS PVAKVVDVTL DGVIPNVAVN
     DGTGAVVGRS SGGVTMVLSP NAIPFTPLEV LPVNSLVGNC ISEEVAGLPF VVSVEELEGK
     TIGLYFGANW YAKCEKFTPL LTEVYQKLKE QGTEFEVVFV SCDEDQSSFE QFHGTMPWVA
     IPFGDLQSRK ILNQRYDIEG IPSLVILSPN GQVLQTNGVE LIRRYGSQAF PFTPLSIREL
     IAEEKANQDS QTLEKLLATN GRDYVIDHGK QVPISNLVGK TIGLFFSALS YPPCAKFTSR
     LASIYRNLRE KHDQFEIVFV SVDKDESSYS QSFSEMPWIA LPYNVESTKL LSRYFDVQGI
     PTLIIIGPDG KTITKEGRNL INLHMEMAYP FTEERLKLLR EKMDEEAKNY PSSLNHAGHR
     HALNLVSENS GGGPFICCEC DEQGLGWAYQ CLGCGYEIHG KCVREVEGKG TSENSPLPKS
     SSGL
//
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