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Database: UniProt
Entry: A0A3N4LVV8_9PEZI
LinkDB: A0A3N4LVV8_9PEZI
Original site: A0A3N4LVV8_9PEZI 
ID   A0A3N4LVV8_9PEZI        Unreviewed;       449 AA.
AC   A0A3N4LVV8;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Saccharopine dehydrogenase {ECO:0000313|EMBL:RPB25322.1};
GN   ORFNames=L211DRAFT_856825 {ECO:0000313|EMBL:RPB25322.1};
OS   Terfezia boudieri ATCC MYA-4762.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Pezizaceae; Terfezia.
OX   NCBI_TaxID=1051890 {ECO:0000313|EMBL:RPB25322.1, ECO:0000313|Proteomes:UP000267821};
RN   [1] {ECO:0000313|EMBL:RPB25322.1, ECO:0000313|Proteomes:UP000267821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4762 {ECO:0000313|EMBL:RPB25322.1,
RC   ECO:0000313|Proteomes:UP000267821};
RX   PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA   Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA   Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA   Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA   Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA   Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA   Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA   Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA   Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA   Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT   "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT   truffle lifestyle.";
RL   Nat. Ecol. Evol. 2:1956-1965(2018).
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DR   EMBL; ML121538; RPB25322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N4LVV8; -.
DR   STRING; 1051890.A0A3N4LVV8; -.
DR   InParanoid; A0A3N4LVV8; -.
DR   Proteomes; UP000267821; Unassembled WGS sequence.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009085; P:lysine biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032095; Sacchrp_dh-like_C.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   PANTHER; PTHR11133:SF25; ALPHA-AMINOADIPIC SEMIALDEHYDE SYNTHASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11133; SACCHAROPINE DEHYDROGENASE; 1.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000267821}.
FT   DOMAIN          6..120
FT                   /note="Saccharopine dehydrogenase NADP binding"
FT                   /evidence="ECO:0000259|Pfam:PF03435"
FT   DOMAIN          124..442
FT                   /note="Saccharopine dehydrogenase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF16653"
SQ   SEQUENCE   449 AA;  49687 MW;  D80F3381C461EF9A CRC64;
     MSTHKVLLLG SGFVAKPCLD ILVKTGIQVT VACRTVETAR KLVGELEGVS PIALDVEDTA
     VLDAEVAKHD LVVSLIPYIH HPIVIKSAIR NKKHVVTTSY VSRAMMELDA QAKAAGITVM
     NEIGLDPGID HLYAVKMIDE VHAAGGKIIS FLSYCGGLPA PEDSDNPLGY KFSWSSRGVL
     LALRNSAKYW KDGKIEEISG PKLMEAAKPY FIYPGYAFIA YPNRDSTEYR ERYNIPEAET
     IIRGTLRYQG FAEFIKAFVD LGFLDDTPVE FLTKTSQPLT WKETVARTLR IESTIEEDLI
     YAISKATTFS NEAEKIRVIN GLRWVGFFSD EKVTPRGNLL DTLCATLEAK MQYGPNERDL
     VMLQHKFEIE LADGKRETRT STLVDYGIPG GYSSMAKLVG VPCGVAVKQI LNGTITDRGV
     LAPMNVKLNN PLIKELKEEY GIECIEKTI
//
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