ID A0A3Q4N417_NEOBR Unreviewed; 291 AA.
AC A0A3Q4N417;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Nucleoredoxin {ECO:0000256|ARBA:ARBA00026178};
DE EC=1.8.1.8 {ECO:0000256|ARBA:ARBA00012612};
OS Neolamprologus brichardi (Fairy cichlid) (Lamprologus brichardi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Lamprologini; Neolamprologus.
OX NCBI_TaxID=32507 {ECO:0000313|Ensembl:ENSNBRP00000026394.1, ECO:0000313|Proteomes:UP000261580};
RN [1] {ECO:0000313|Ensembl:ENSNBRP00000026394.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) 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 AlphaFoldDB; A0A3Q4N417; -.
DR STRING; 32507.ENSNBRP00000026394; -.
DR Ensembl; ENSNBRT00000027094.1; ENSNBRP00000026394.1; ENSNBRG00000020162.1.
DR GeneTree; ENSGT00940000161894; -.
DR OMA; HEDQELF; -.
DR Proteomes; UP000261580; Unplaced.
DR Bgee; ENSNBRG00000020162; Expressed in brain and 2 other cell types or tissues.
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; 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; 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:UP000261580}.
FT DOMAIN 8..182
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 291 AA; 33002 MW; 54CFB506A0B10E69 CRC64;
MFPLSLPPLL SYPLSGLEFP WGPKPFAEVV AGPLLRNNRQ TTDSSSLEGH YVGVYFSAHW
CPPCRSLTRV LVESYRTVKE SGQKFEIVFV SADRSEESFK QYFSEMPWLA VPYSDEARRS
RLNRLYGIQG IPTLILLDTE GHMITRQGRV EVLNDPECRL FPWHPRPVLE LSESNAVQLH
EGPCLVLFVD AEEEGELEPA KELIQPIAEK LMAKYKAKEE ETPLLFFVAG EDDMSDSLRD
YTNLPEAAPL LTILDMSARA KYVRDVEEIT PAVVEQFVGD FLAEKLKPEP I
//
