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Database: UniProt
Entry: A0A3Q0RVS0_AMPCI
LinkDB: A0A3Q0RVS0_AMPCI
Original site: A0A3Q0RVS0_AMPCI 
ID   A0A3Q0RVS0_AMPCI        Unreviewed;       440 AA.
AC   A0A3Q0RVS0;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Thioredoxin reductase 2, tandem duplicate 1 {ECO:0000313|Ensembl:ENSACIP00000012375.1};
GN   Name=TXNRD2 {ECO:0000313|Ensembl:ENSACIP00000012375.1};
OS   Amphilophus citrinellus (Midas cichlid) (Cichlasoma citrinellum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; New World cichlids;
OC   Cichlasomatinae; Heroini; Amphilophus.
OX   NCBI_TaxID=61819 {ECO:0000313|Ensembl:ENSACIP00000012375.1, ECO:0000313|Proteomes:UP000261340};
RN   [1] {ECO:0000313|Ensembl:ENSACIP00000012375.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
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DR   AlphaFoldDB; A0A3Q0RVS0; -.
DR   Ensembl; ENSACIT00000012722.1; ENSACIP00000012375.1; ENSACIG00000009370.1.
DR   GeneTree; ENSGT00940000158832; -.
DR   Proteomes; UP000261340; Unplaced.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF3; THIOREDOXIN-DISULFIDE REDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691}.
FT   DOMAIN          38..333
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          353..438
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   440 AA;  48207 MW;  D61CAE307F59E817 CRC64;
     MAAFCRGRHR WKKINCLHIF SRKLTGKVRL FSLGKYDYDM LVIGGGSGGL ACSKEGTKWG
     LGGTCVNVGC IPKKLMHQAA LLGTAVKDLN YSVAVQNHVK SLNWGHRVQL QDKKVKYMNL
     KGSLVDEHTV RGLNKAGKET ILTAKNIVIA TGGRPKYPTN IPGAVEHGIT SDDIFWLKKS
     PGKTYCSLNK LLHILGVVVE IFVMFEFGCP PFLFVQQMAG LVTDYMEAYG TRFAWKSVPN
     RVDKLPSGAL QVTWTNTQTG GEHKDTFDCV LWAVGRAPET KALGLDKLGI QLNKETGKII
     VGADESASVP NIYAFGDIGE GRPELTPTAI KAGKLLARRL AGQSAELMNY DNVPTTVFTP
     LEYSCVGLSE EEAEKRHGKD RIEVYHAFYK PLEFTVAERD ASQCYIKVVC ERGGNGKILG
     LHFTGPNAGE VAQGFAMSFQ
//
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