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Database: UniProt
Entry: A0A0F4GX29_9PEZI
LinkDB: A0A0F4GX29_9PEZI
Original site: A0A0F4GX29_9PEZI 
ID   A0A0F4GX29_9PEZI        Unreviewed;       375 AA.
AC   A0A0F4GX29;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   07-NOV-2018, entry version 16.
DE   RecName: Full=Saccharopine dehydrogenase [NAD(+), L-lysine-forming] {ECO:0000256|PIRNR:PIRNR018250};
DE            Short=SDH {ECO:0000256|PIRNR:PIRNR018250};
DE            EC=1.5.1.7 {ECO:0000256|PIRNR:PIRNR018250};
DE   AltName: Full=Lysine--2-oxoglutarate reductase {ECO:0000256|PIRNR:PIRNR018250};
GN   ORFNames=TI39_contig266g00001 {ECO:0000313|EMBL:KJY01975.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Dothideomycetes; Dothideomycetidae; Capnodiales; Mycosphaerellaceae;
OC   Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY01975.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJY01975.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJY01975.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related
RT   genes and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+)
CC       + H(2)O = L-lysine + 2-oxoglutarate + NADH.
CC       {ECO:0000256|PIRNR:PIRNR018250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-lysine from L-alpha-aminoadipate (fungal route): step
CC       3/3. {ECO:0000256|PIRNR:PIRNR018250}.
CC   -!- SIMILARITY: Belongs to the AlaDH/PNT family.
CC       {ECO:0000256|PIRNR:PIRNR018250}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KJY01975.1}.
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DR   EMBL; LAFY01000258; KJY01975.1; -; Genomic_DNA.
DR   EnsemblFungi; KJY01975; KJY01975; TI39_contig266g00001.
DR   UniPathway; UPA00033; UER00034.
DR   Proteomes; UP000033647; Unassembled WGS sequence.
DR   GO; GO:0004754; F:saccharopine dehydrogenase (NAD+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR   CDD; cd12188; SDH; 1.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR   InterPro; IPR027281; Lys1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR11133:SF15; PTHR11133:SF15; 1.
DR   Pfam; PF01262; AlaDh_PNT_C; 1.
DR   Pfam; PF05222; AlaDh_PNT_N; 1.
DR   PIRSF; PIRSF018250; Saccharopine_DH_Lys; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR018250};
KW   Complete proteome {ECO:0000313|Proteomes:UP000033647};
KW   Lysine biosynthesis {ECO:0000256|PIRNR:PIRNR018250};
KW   NAD {ECO:0000256|PIRNR:PIRNR018250};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR018250};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT   DOMAIN        9    143       AlaDh_PNT_N. {ECO:0000259|SMART:SM01003}.
FT   DOMAIN      179    320       AlaDh_PNT_C. {ECO:0000259|SMART:SM01002}.
FT   ACT_SITE    206    206       {ECO:0000256|PIRSR:PIRSR018250-1}.
SQ   SEQUENCE   375 AA;  41079 MW;  EC22334B7A0CDAB7 CRC64;
     MSSSPLTLHI RAETKPLEHR TAVPPKVARK LVEAGYVVNV ERSPLSIFPD NEYEGRGATL
     VPTGSWTEAP KEHIIVGLKE LPEEDFALVH THVQFAHCYK NQGGWEKVLS RFPRGGGTLL
     DLEFLEDEQG RRVAAFGYHA GFAGAALSLI AWAWQLEHGT SKPVPGVTAY ENETLLVNDV
     KKAVEKGKSI AGHLPRVLVI GALGRCGRGA VDLCVKAGLQ DILKWDLQET KAKPGPYQEI
     IESDVFVNCI YLSAKIPPFI DAPSLASPTR KLSVVCDVSC DTTNPHNPIP IYSINTTFDK
     PTVPVELSSE ANDVPLSVIS IDHLPSLLPR EASEAFSEAL LPSLLELKER KTARVWRQAE
     KLFEDKVASL PKGSY
//
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