GenomeNet

Database: UniProt
Entry: F0Y8N6_AURAN
LinkDB: F0Y8N6_AURAN
Original site: F0Y8N6_AURAN 
ID   F0Y8N6_AURAN            Unreviewed;       482 AA.
AC   F0Y8N6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Uncharacterized protein DLD1 {ECO:0000313|EMBL:EGB08685.1};
GN   Name=DLD1 {ECO:0000313|EMBL:EGB08685.1};
GN   ORFNames=AURANDRAFT_25795 {ECO:0000313|EMBL:EGB08685.1};
OS   Aureococcus anophagefferens (Harmful bloom alga).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Pelagophyceae; Pelagomonadales;
OC   Aureococcus.
OX   NCBI_TaxID=44056 {ECO:0000313|Proteomes:UP000002729};
RN   [1] {ECO:0000313|EMBL:EGB08685.1, ECO:0000313|Proteomes:UP000002729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP 1984 {ECO:0000313|Proteomes:UP000002729};
RX   PubMed=21368207; DOI=10.1073/pnas.1016106108;
RA   Gobler C.J., Berry D.L., Dyhrman S.T., Wilhelm S.W., Salamov A.,
RA   Lobanov A.V., Zhang Y., Collier J.L., Wurch L.L., Kustka A.B., Dill B.D.,
RA   Shah M., VerBerkmoes N.C., Kuo A., Terry A., Pangilinan J., Lindquist E.A.,
RA   Lucas S., Paulsen I.T., Hattenrath-Lehmann T.K., Talmage S.C., Walker E.A.,
RA   Koch F., Burson A.M., Marcoval M.A., Tang Y.Z., Lecleir G.R., Coyne K.J.,
RA   Berg G.M., Bertrand E.M., Saito M.A., Gladyshev V.N., Grigoriev I.V.;
RT   "Niche of harmful alga Aureococcus anophagefferens revealed through
RT   ecogenomics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:4352-4357(2011).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC       ECO:0000256|RuleBase:RU003691}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GL833127; EGB08685.1; -; Genomic_DNA.
DR   RefSeq; XP_009036675.1; XM_009038427.1.
DR   AlphaFoldDB; F0Y8N6; -.
DR   EnsemblProtists; EGB08685; EGB08685; AURANDRAFT_25795.
DR   GeneID; 20220105; -.
DR   KEGG; aaf:AURANDRAFT_25795; -.
DR   eggNOG; KOG1335; Eukaryota.
DR   InParanoid; F0Y8N6; -.
DR   OMA; WASMLND; -.
DR   OrthoDB; 203590at2759; -.
DR   Proteomes; UP000002729; Unassembled WGS sequence.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PANTHER; PTHR22912:SF151; 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   PIRSF; PIRSF000350; Mercury_reductase_MerA; 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|PIRSR:PIRSR000350-3};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003691};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW   ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002729}.
FT   DOMAIN          6..341
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          360..470
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   ACT_SITE        462
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT   BINDING         52
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         119
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         181..188
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         278
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         326
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   BINDING         332..335
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT   DISULFID        43..48
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ   SEQUENCE   482 AA;  50440 MW;  E71D7253B4696022 CRC64;
     MHDFDYDVVI VGCGVGGHGA ALHARSQGLS CAVLSGGDVG GTCVNRGCVP SKALLAASGR
     VRDMGDEKHL ESMGITVPGG VEFDRAGIAA HAEQLVNKVR GGLEGSLGRL GVELIPEFGA
     YGGPNTVELG NGKKVTAQDI ILAPGSVPFV PPGVTIDGET VYTSDEGLRL EHVPEYCAII
     GSGIIGLEFS DVYTALGSEC TLIEALPKLM PAFDREIAKQ AERLLLTPRG IDYRTGVFAS
     KVTPGKLGEK PVVIEMIDAE TKELVEVLEV DTCMVATGRV PNTGKLGLDK HGIETPRGFV
     QVDETMRVLA GPGGAVADEH LYCIGDANGI QMLAHTASTQ GVSAIENICG RKHVVNHEDI
     PAACFTHPEV AQVGIDEDAA KDRAEAEGFE LGKAVGHFRA NSKALAEGEG DGIAKVLFNK
     DTEQILGVHI IGLHAADLIQ ECANAKAAGT TVRELAFTTH THPTLSEVID GAFKECVGMH
     AH
//
DBGET integrated database retrieval system