ID   A0A493TGV2_ANAPP        Unreviewed;       879 AA.
AC   A0A493TGV2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Aminoadipate-semialdehyde synthase {ECO:0000313|Ensembl:ENSAPLP00000025117.1};
GN   Name=AASS {ECO:0000313|Ensembl:ENSAPLP00000025117.1};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000025117.1, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000025117.1, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000025117.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 1/6.
CC       {ECO:0000256|ARBA:ARBA00004682}.
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC       pathway; glutaryl-CoA from L-lysine: step 2/6.
CC       {ECO:0000256|ARBA:ARBA00004720}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC       dehydrogenase family. {ECO:0000256|ARBA:ARBA00025744}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC       {ECO:0000256|ARBA:ARBA00005624}.
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DR   AlphaFoldDB; A0A493TGV2; -.
DR   Ensembl; ENSAPLT00000026914.1; ENSAPLP00000025117.1; ENSAPLG00000015230.2.
DR   GeneTree; ENSGT00390000013249; -.
DR   UniPathway; UPA00868; UER00835.
DR   Proteomes; UP000016666; Chromosome 1.
DR   GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR   CDD; cd12189; LKR_SDH_like; 1.
DR   Gene3D; 1.10.1870.10; Domain 3, Saccharopine reductase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 4.
DR   InterPro; IPR007886; AlaDH/PNT_N.
DR   InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
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; PF05222; AlaDh_PNT_N; 1.
DR   Pfam; PF16653; Sacchrp_dh_C; 1.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SMART; SM01002; AlaDh_PNT_C; 1.
DR   SMART; SM01003; AlaDh_PNT_N; 1.
DR   SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016666}.
FT   DOMAIN          28..158
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          198..400
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   879 AA;  97904 MW;  2622A9279B5B06D9 CRC64;
     MLRAFSHTNG KCAFRHAKCR YHHKSVLAIR REDVNAWERR APLAPKHVKE LTQMGYKVLV
     QPSNRRAIHE KDYVKAGGII QEDISEASLI VGVKRPPEDK LIPKKNYAFF SHTIKAQEAN
     MPLLDEILRQ EIRLFDYEKM VDHKGMRVVA FGKWAGVAGM INILHGLGLR FLALGHHTPF
     MHIGMAHNYR NSSQAVQAVR DAGYEISLGL MPKSVGPLTF VFTGTGNVSK GAQEMFNALP
     CEFVEPHELK EVSQSGDLRK VYGTVLSRHH HLVRKHDGMY DPVDYDKHPE LYTSRFNTDI
     APYTTCLING IYWEQHTPRL LSRQDAQKLL MPVRSAAGAP EGCPELPHKL LAICDISADT
     GGSIEFMTEC TTIDSPFCMY DADQHIIHDS VEGSGILMCS IDNLPAQLPI EATEYFGDML
     FPYIEEMLLS EGSEPLEKQN YSSVVRDAVI ASNGSLTAKY EYIQKLRESR EYAQNMDNKK
     RVLVLGSGYV SGPVLEYLTR DSNVDITIAS VMEEQLEQLT EKFSNVTSVH MDVLKHEEKL
     SSLVKKHDLV ISLLPYSAHP LVAKKCINNK VNLVTASYLT PAMKELQKSV EAAGITVISE
     VGLDPGLDHM LAMECIDKAK EVGATVINIP AGGALLDSVS PMDFFPGLNL EGFPNRDSTK
     YAEPYGIQTA HTLLRGTLRY KGYSKTMGGF VKLGLINPDP YPLLNSDAPR LTWKQLMCKL
     VGIQPPVEYS VLREAVFNKL ERDKSQLEAV EWLGLLGDEP VPTADSIVGA LAKHMEMNLP
     FGTGERDMIV MRNEIGLRHP SGHLEDKFID LVVYGDNKGY SAMAKTVGYP TAIAAKMVLD
     GEIDVKGMVI PLTKNIYGPI LERVRAEGIV YSTHSVIRQ
//