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Database: UniProt
Entry: B7FWJ3_PHATC
LinkDB: B7FWJ3_PHATC
Original site: B7FWJ3_PHATC 
ID   B7FWJ3_PHATC            Unreviewed;       427 AA.
AC   B7FWJ3;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Oxidoreductase FAD/NAD(P)-binding domain-containing protein {ECO:0000259|Pfam:PF00175};
GN   ORFNames=PHATRDRAFT_45124 {ECO:0000313|EMBL:EEC48993.1};
OS   Phaeodactylum tricornutum (strain CCAP 1055/1).
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Bacillariophyceae; Bacillariophycidae; Naviculales; Phaeodactylaceae;
OC   Phaeodactylum.
OX   NCBI_TaxID=556484 {ECO:0000313|EMBL:EEC48993.1, ECO:0000313|Proteomes:UP000000759};
RN   [1] {ECO:0000313|EMBL:EEC48993.1, ECO:0000313|Proteomes:UP000000759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCAP 1055/1 {ECO:0000313|EMBL:EEC48993.1,
RC   ECO:0000313|Proteomes:UP000000759};
RX   PubMed=18923393; DOI=10.1038/nature07410;
RA   Bowler C., Allen A.E., Badger J.H., Grimwood J., Jabbari K., Kuo A.,
RA   Maheswari U., Martens C., Maumus F., Otillar R.P., Rayko E., Salamov A.,
RA   Vandepoele K., Beszteri B., Gruber A., Heijde M., Katinka M., Mock T.,
RA   Valentin K., Verret F., Berges J.A., Brownlee C., Cadoret J.P.,
RA   Chiovitti A., Choi C.J., Coesel S., De Martino A., Detter J.C., Durkin C.,
RA   Falciatore A., Fournet J., Haruta M., Huysman M.J., Jenkins B.D.,
RA   Jiroutova K., Jorgensen R.E., Joubert Y., Kaplan A., Kroger N., Kroth P.G.,
RA   La Roche J., Lindquist E., Lommer M., Martin-Jezequel V., Lopez P.J.,
RA   Lucas S., Mangogna M., McGinnis K., Medlin L.K., Montsant A.,
RA   Oudot-Le Secq M.P., Napoli C., Obornik M., Parker M.S., Petit J.L.,
RA   Porcel B.M., Poulsen N., Robison M., Rychlewski L., Rynearson T.A.,
RA   Schmutz J., Shapiro H., Siaut M., Stanley M., Sussman M.R., Taylor A.R.,
RA   Vardi A., von Dassow P., Vyverman W., Willis A., Wyrwicz L.S.,
RA   Rokhsar D.S., Weissenbach J., Armbrust E.V., Green B.R., Van de Peer Y.,
RA   Grigoriev I.V.;
RT   "The Phaeodactylum genome reveals the evolutionary history of diatom
RT   genomes.";
RL   Nature 456:239-244(2008).
RN   [2] {ECO:0000313|Proteomes:UP000000759}
RP   GENOME REANNOTATION.
RC   STRAIN=CCAP 1055/1 {ECO:0000313|Proteomes:UP000000759};
RG   Diatom Consortium;
RA   Grigoriev I., Grimwood J., Kuo A., Otillar R.P., Salamov A., Detter J.C.,
RA   Lindquist E., Shapiro H., Lucas S., Glavina del Rio T., Pitluck S.,
RA   Rokhsar D., Bowler C.;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR601834-1};
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DR   EMBL; CM000609; EEC48993.1; -; Genomic_DNA.
DR   RefSeq; XP_002179170.1; XM_002179134.1.
DR   AlphaFoldDB; B7FWJ3; -.
DR   PaxDb; 2850-Phatr45124; -.
DR   EnsemblProtists; Phatr3_J45124.t1; Phatr3_J45124.p1; Phatr3_J45124.
DR   GeneID; 7200189; -.
DR   KEGG; pti:PHATRDRAFT_45124; -.
DR   eggNOG; ENOG502S7AX; Eukaryota.
DR   HOGENOM; CLU_616110_0_0_1; -.
DR   InParanoid; B7FWJ3; -.
DR   OMA; NCICVLP; -.
DR   OrthoDB; 5624322at2759; -.
DR   Proteomes; UP000000759; Chromosome 6.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   InterPro; IPR001834; CBR-like.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   PANTHER; PTHR19370; NADH-CYTOCHROME B5 REDUCTASE; 1.
DR   PANTHER; PTHR19370:SF185; NADH-CYTOCHROME B5 REDUCTASE 2; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|PIRSR:PIRSR601834-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR601834-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000759};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..427
FT                   /note="Oxidoreductase FAD/NAD(P)-binding domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002855533"
FT   DOMAIN          307..409
FT                   /note="Oxidoreductase FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00175"
FT   REGION          38..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
FT   BINDING         249
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601834-1"
SQ   SEQUENCE   427 AA;  46537 MW;  FBF7667A2AD432EE CRC64;
     MKEGPRRRRR QSVEILYLSL VAGSSAVSAF QPLHAQSRTY PRRTSLPGPP RKRTSSVEVQ
     MSSPGVRVPR ASVRVAIDQP LISDTFFTKG AAAKATARTG ILQTVTGALS AISLRTVLTT
     VFVALLATIL VRSSSSIAET LGKTFRLVSG RVQRVWERFQ RVDEGIPMPF DEKANDGWGI
     CTLKSKERLG KSNFMQYTFD LPEPDYVLPL DLGQQISMMC LDDDGDVAQG DFFSYNLSAS
     PKPGSFTILF PTGSHEENTC SIGSSGANFL RALKQDVKVG DEIALKPGPI KLSYRGQYLP
     VTGMVYIACG TGIVPVLDQV RAVLPADSSS VTSVSVVWIN EEAKDFDVTA ELLEKEYYKY
     SKKLAVSCVV DNTMQRQSLG DNTEVHAAVP DFTQGTMAVI AGPSDMAKKA IAFLENRGYP
     RDTICVL
//
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