ID C5DWU2_ZYGRC Unreviewed; 446 AA.
AC C5DWU2;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=ZYRO0D17578p {ECO:0000313|EMBL:CAR28261.1};
GN OrderedLocusNames=ZYRO0D17578g {ECO:0000313|EMBL:CAR28261.1};
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307 {ECO:0000313|EMBL:CAR28261.1, ECO:0000313|Proteomes:UP000008536};
RN [1] {ECO:0000313|Proteomes:UP000008536}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229 {ECO:0000313|Proteomes:UP000008536};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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DR EMBL; CU928176; CAR28261.1; -; Genomic_DNA.
DR RefSeq; XP_002497194.1; XM_002497149.1.
DR AlphaFoldDB; C5DWU2; -.
DR STRING; 559307.C5DWU2; -.
DR GeneID; 8204464; -.
DR KEGG; zro:ZYRO0D17578g; -.
DR HOGENOM; CLU_016207_3_1_1; -.
DR InParanoid; C5DWU2; -.
DR Proteomes; UP000008536; Chromosome D.
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:UP000008536}.
FT DOMAIN 5..119
FT /note="Saccharopine dehydrogenase NADP binding"
FT /evidence="ECO:0000259|Pfam:PF03435"
FT DOMAIN 123..438
FT /note="Saccharopine dehydrogenase-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16653"
SQ SEQUENCE 446 AA; 49110 MW; CEC305ED626980EA CRC64;
MVKNVLLLGS GFVAQPVVDS LAAEKDINVT VACRTLAKAE ALAKPSKSAS ASVDVTNDSQ
LDSLLEKNDL VISLIPYIYH PNVVKSAIRT KTNVLTTSYI SPALRELEPE IKKAGILVMN
EIGLDPGIDH LYAVKTIDEV HKVGGKIKSF LSFCGGLPAP EDSDNPLGYK FSWSSRGVLL
ALRNTAKFWR DGKVEVVSSE DLMATAKPYF IYPGFAFVAY PNRDSTVFKE LYEIPEAETV
IRGTLRYQGF PEFVKALVDI NFLSEDPESA FTKALPWKEA LKQFLGASSS SKEDLVKVID
SKTKWQSEED RARILAGFNW LGFFSDILIT PKGNPLDTLC ARLEELMQYE EGERDLVVLQ
HKFGIEWADG STETRTSTLV DYGKVGGYSS MAATVGYPAS IAAKLIFDGV IKGSGLRAPY
SPEINDPIMK NLKDKYGIYM KEKTIA
//
