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Database: UniProt
Entry: A0A395MT46_9HYPO
LinkDB: A0A395MT46_9HYPO
Original site: A0A395MT46_9HYPO 
ID   A0A395MT46_9HYPO        Unreviewed;       422 AA.
AC   A0A395MT46;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   SubName: Full=Saccharopine dehydrogenase {ECO:0000313|EMBL:RFN50349.1};
GN   ORFNames=FIE12Z_5383 {ECO:0000313|EMBL:RFN50349.1};
OS   Fusarium flagelliforme.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium incarnatum-equiseti species complex.
OX   NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN50349.1, ECO:0000313|Proteomes:UP000265631};
RN   [1] {ECO:0000313|EMBL:RFN50349.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN50349.1};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00038048}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RFN50349.1}.
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DR   EMBL; PXXK01000141; RFN50349.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395MT46; -.
DR   OrthoDB; 5479972at2759; -.
DR   Proteomes; UP000265631; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   PANTHER; PTHR12286:SF5; SACCHAROPINE DEHYDROGENASE-LIKE OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR12286; UNCHARACTERIZED; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..142
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
SQ   SEQUENCE   422 AA;  45936 MW;  C7F028A925875FB6 CRC64;
     MPLLKDHGRQ YDVVVFGATG YTGKLTAEYI TTHLSTDLKW AVAGRNESKL KAVVEDCKKL
     NPDRLAPAIE IANLNDQELS GLAKKTCVLL TTVGPYSLYG EHAYKACAEA GTHYVDVTGE
     AAWVHKMIKK YEATAKKTGA ILIPQAGIES SPADLSTWAL AKAIRTELGS QTKDVTISLH
     EVNSSPSGGT LATALSIWDV FTLNEIKEAS SPYAQSPVPH KEPKRPKSSI LQMILGVGSV
     PNLGLLTTSV AGSTDVAVVE RTWGLLSETP SRKEEFYGPN FVWQERMKAR NWLHGIFIHW
     LLVIGGVLLV SVAPLREFLK KRVVQPGQGA NREETAKDYV EYRGIAHPDS KEHAGKAAFS
     RMWHHGGMYL LTAVLLGEIA ATILEDPIEL DGGSYTPACL GQGLIDRLDK SGLKLDVKII
     DE
//
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