ID C3NG34_SULIN Unreviewed; 409 AA.
AC C3NG34;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=FAD-dependent pyridine nucleotide-disulphideoxido reductase {ECO:0000313|EMBL:ACP49995.1};
GN OrderedLocusNames=YN1551_3112 {ECO:0000313|EMBL:ACP49995.1};
OS Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=419942 {ECO:0000313|EMBL:ACP49995.1, ECO:0000313|Proteomes:UP000006818};
RN [1] {ECO:0000313|EMBL:ACP49995.1, ECO:0000313|Proteomes:UP000006818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y.N.15.51 / Yellowstone #2 {ECO:0000313|Proteomes:UP000006818};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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 EMBL; CP001404; ACP49995.1; -; Genomic_DNA.
DR RefSeq; WP_012716879.1; NC_012623.1.
DR AlphaFoldDB; C3NG34; -.
DR GeneID; 7811307; -.
DR KEGG; sin:YN1551_3112; -.
DR HOGENOM; CLU_016755_0_3_2; -.
DR Proteomes; UP000006818; Chromosome.
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 Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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 InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 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}; NAD {ECO:0000256|ARBA:ARBA00023027};
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 1..289
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 308..405
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 409 AA; 45132 MW; 4EA56C1F40DBE150 CRC64;
MKVAVIGSGP AGIDASLELA KNNKVILVEK EERLGGTCVL YGCIPSKAML HPIHLASELE
KLGKSIVFDL GELRKLGQEA SFRLSKGVEY MLEDNGVEVI YGVASLRSGQ LNVNNETLQT
DYIVLATGTY REVVKGIIYS EDLPYLDKDF QSVVIVGGDV GGVEFGWMLR KLGKEVVIID
KQSSLLPYLD KEVSNAITNY FSKIGMKLYL NRSVKEMKER EVVLENGERL TADVVYMTFG
RKPSIQGFEE VNHNPFVTVD EYLRTSISNV FAAGDIIGTH TAHEAMYAGK VAAINVMGGK
KVFNKQGIPK VVYTHPTIAY VGNMEGKCAK INLAEIGRAI TEKETDGFLK ICVKDDKIVG
AQAFMKDAEE VISLISFLIR YNIKVSEIKD YVAPHPSYIE AITELLSRL
//
