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
//