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Database: UniProt
Entry: M5FU01_DACPD
LinkDB: M5FU01_DACPD
Original site: M5FU01_DACPD 
ID   M5FU01_DACPD            Unreviewed;       350 AA.
AC   M5FU01;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=NADP-binding protein {ECO:0000313|EMBL:EJT99638.1};
GN   ORFNames=DACRYDRAFT_117835 {ECO:0000313|EMBL:EJT99638.1};
OS   Dacryopinax primogenitus (strain DJM 731) (Brown rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC   Dacrymycetales; Dacrymycetaceae; Dacryopinax.
OX   NCBI_TaxID=1858805 {ECO:0000313|EMBL:EJT99638.1, ECO:0000313|Proteomes:UP000030653};
RN   [1] {ECO:0000313|EMBL:EJT99638.1, ECO:0000313|Proteomes:UP000030653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJM-731 SS1 {ECO:0000313|EMBL:EJT99638.1,
RC   ECO:0000313|Proteomes:UP000030653};
RX   PubMed=22745431; DOI=10.1126/science.1221748;
RA   Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA   Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA   Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA   Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA   Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA   Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA   Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA   Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA   Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA   Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA   Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA   Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA   Hibbett D.S.;
RT   "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT   31 fungal genomes.";
RL   Science 336:1715-1719(2012).
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. Dihydroflavonol-4-reductase subfamily.
CC       {ECO:0000256|ARBA:ARBA00023445}.
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DR   EMBL; JH795869; EJT99638.1; -; Genomic_DNA.
DR   AlphaFoldDB; M5FU01; -.
DR   STRING; 1858805.M5FU01; -.
DR   HOGENOM; CLU_007383_9_2_1; -.
DR   OMA; NEEWYFL; -.
DR   OrthoDB; 987679at2759; -.
DR   Proteomes; UP000030653; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR10366:SF849; FATTY ACID HYDROXYLASE UHD1; 1.
DR   PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030653}.
FT   DOMAIN          10..268
FT                   /note="NAD-dependent epimerase/dehydratase"
FT                   /evidence="ECO:0000259|Pfam:PF01370"
SQ   SEQUENCE   350 AA;  38280 MW;  A523FE7AD9417AAE CRC64;
     MVAVQPPALV LVTGASGFLA AHACQTLLEK EFKVRGTVRS KEKGEYLVNL YKNSNFSYTI
     VPDIRPPNAF DEAVKGVDAV LHMASPFQVN VVDPEDLVRP AVQGTKGVLE SIQTFNCVTI
     IPSVKRVIIT SSIASITVPS EPGHVFTETD WNTLSADIVA REGINAPGME KYRLSKVSAE
     RAAWEFVDGQ KPTWDLVTVC PLMIYRTIIH ECASVERLNT SIAQLRVAFT PEGAKRGEDA
     GRQAGNWADV RDVAEIHTQA LLQQKAGGNR FIAGGGPFSW QMMYDSVQAF GHIDGLDVDQ
     LPKGTPGSDR NTVYMVTSNE KAKRELGIKF HLMGECVRDT LLSLKALGFF
//
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