ID A0A087R009_APTFO Unreviewed; 319 AA.
AC A0A087R009;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=Nucleoredoxin {ECO:0000256|ARBA:ARBA00026178};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
DE Flags: Fragment;
GN ORFNames=AS27_13490 {ECO:0000313|EMBL:KFM06813.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM06813.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM06813.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM06813.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KL226004; KFM06813.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087R009; -.
DR STRING; 9233.A0A087R009; -.
DR Proteomes; UP000053286; Unassembled WGS sequence.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase (NADP) activity; IEA:InterPro.
DR CDD; cd03071; PDI_b'_NRX; 1.
DR CDD; cd03009; TryX_like_TryX_NRX; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 3.
DR InterPro; IPR041861; NRX_PDI_b.
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; PTHR46472; NUCLEOREDOXIN; 1.
DR PANTHER; PTHR46472:SF1; NUCLEOREDOXIN; 1.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR Pfam; PF13905; Thioredoxin_8; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT DOMAIN 48..186
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM06813.1"
FT NON_TER 319
FT /evidence="ECO:0000313|EMBL:KFM06813.1"
SQ SEQUENCE 319 AA; 35876 MW; 63305307D8F0A96B CRC64;
SLLQLKLWNK YRVSNIPSLI FIDASTGKVV CRNGLLVIRD DPEGLEFPWG PKPFSEVVAG
PLLRNNGQTL DSNALEGSHV GVYFSAHWCP PCRSLTRVLV ESYRKIKEAG QKFEILFVSA
DRSEDSFKQY FSEMPWVAVP YADEARRSRL NRLYGIQGIP TLIVLDSKGD VITRQGRVEV
LNDIECREFP WHPKPVLELT DSNAVQLNEG PCLVLFVDSE DDGESEAAKQ LIQPIAEKII
AKYKAKEEEA PLLFFVAGED DMTDSLRDYT NLPEAAPLLT ILDMSARAKY VMDVEEITPE
IVEAFVSDFL ADKLKPEPI
//
