ID C5A5P0_THEGJ Unreviewed; 441 AA.
AC C5A5P0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=NAD(P)H sulfur oxidoreductase {ECO:0000313|EMBL:ACS33552.1};
DE EC=1.6.99.3 {ECO:0000313|EMBL:ACS33552.1};
GN OrderedLocusNames=TGAM_1050 {ECO:0000313|EMBL:ACS33552.1};
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117 {ECO:0000313|EMBL:ACS33552.1, ECO:0000313|Proteomes:UP000001488};
RN [1] {ECO:0000313|EMBL:ACS33552.1, ECO:0000313|Proteomes:UP000001488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3
RC {ECO:0000313|Proteomes:UP000001488};
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130}.
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DR EMBL; CP001398; ACS33552.1; -; Genomic_DNA.
DR RefSeq; WP_015858666.1; NC_012804.1.
DR AlphaFoldDB; C5A5P0; -.
DR STRING; 593117.TGAM_1050; -.
DR PaxDb; 593117-TGAM_1050; -.
DR GeneID; 7986924; -.
DR KEGG; tga:TGAM_1050; -.
DR PATRIC; fig|593117.10.peg.1047; -.
DR eggNOG; arCOG01069; Archaea.
DR HOGENOM; CLU_003291_1_3_2; -.
DR OrthoDB; 27922at2157; -.
DR Proteomes; UP000001488; Chromosome.
DR GO; GO:0050451; F:CoA-disulfide reductase (NADP) activity; IEA:InterPro.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR017758; CoA_disulphide_reductase.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR NCBIfam; TIGR03385; CoA_CoA_reduc; 1.
DR PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000313|EMBL:ACS33552.1}.
FT DOMAIN 3..297
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 326..428
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 441 AA; 48327 MW; 38E53FE6EA531890 CRC64;
MGKKVVIIGG GAAGMSTASR VKRLKPEWDV KVFEATEWVS HAPCGIPYVV EGISPTEKLM
HYPPEVFIKK RGIDLHLKAE VIEVGQGYVR VREGDGEKSY EWDYLVFANG ASPRIPAVEG
VTLPGVFKAD LPPDAVAIKE YIEKNRVEDV VIIGGGYIGV EMAEAFSAQG KNVTLIERNE
RVMSKAFDRE ITDVLEEEMR KRIDLRTQEI VLKIEGSERV EKVITDAGEY KADLVILATG
IKPNVELAKE IGVRIGETGA IWTNEKMQTS VENVYAAGDV AETRHLITGR RVWIPLAPAG
NKMGYVAGSN IAGKELHFPG VLGTSVTKFF DVEIGKTGLT EAEAIREGYD VRTAFIKATT
RPHYYPGAKP IWLKGVVDNE TNRLLGVQAV GAEILPRIDT AAAMLTAGFT TKDAFFTDLA
YAPPFAPVWD PLVVLARVLK F
//
