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Database: UniProt
Entry: C5M1M2_PERM5
LinkDB: C5M1M2_PERM5
Original site: C5M1M2_PERM5 
ID   C5M1M2_PERM5            Unreviewed;       127 AA.
AC   C5M1M2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-NOV-2023, entry version 48.
DE   SubName: Full=Glutathione reductase, putative {ECO:0000313|EMBL:EEQ97120.1};
DE   Flags: Fragment;
GN   ORFNames=Pmar_PMAR017241 {ECO:0000313|EMBL:EEQ97120.1};
OS   Perkinsus marinus (strain ATCC 50983 / TXsc).
OC   Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC   Perkinsus.
OX   NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN   [1] {ECO:0000313|EMBL:EEQ97120.1, ECO:0000313|Proteomes:UP000007800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA   El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; GG687559; EEQ97120.1; -; Genomic_DNA.
DR   RefSeq; XP_002764403.1; XM_002764357.1.
DR   AlphaFoldDB; C5M1M2; -.
DR   EnsemblProtists; EEQ97120; EEQ97120; Pmar_PMAR017241.
DR   GeneID; 9053442; -.
DR   InParanoid; C5M1M2; -.
DR   OrthoDB; 5473641at2759; -.
DR   Proteomes; UP000007800; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase (NADP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR046952; GSHR/TRXR-like.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR   PANTHER; PTHR42737:SF2; GLUTATHIONE REDUCTASE; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT   DOMAIN          4..118
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EEQ97120.1"
SQ   SEQUENCE   127 AA;  13856 MW;  11A3FAE6FB1EE3F0 CRC64;
     YETIPTVVFA HPPIGTCGLT EAQAVEKYGK DNLKIYRSRF VNLYYGIFQV EPSDKPKTLV
     KVICTGPEEK VVGLHVIGMA ADELLQGFAV AMRMGATKAD LDRTVAIHPT AGEEIVTLAP
     WGPMSKH
//
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