ID   A0A287B8T1_PIG          Unreviewed;       823 AA.
AC   A0A287B8T1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Aminoadipate-semialdehyde synthase {ECO:0000313|Ensembl:ENSSSCP00000052487.1};
GN   Name=AASS {ECO:0000313|Ensembl:ENSSSCP00000052487.1,
GN   ECO:0000313|VGNC:VGNC:84944};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000052487.1, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000052487.1, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000052487.1,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000052487.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A287B8T1; -.
DR   Ensembl; ENSSSCT00000056868.2; ENSSSCP00000052487.1; ENSSSCG00000016613.5.
DR   VGNC; VGNC:84944; AASS.
DR   GeneTree; ENSGT00390000013249; -.
DR   UniPathway; UPA00868; UER00835.
DR   Proteomes; UP000008227; Chromosome 18.
DR   Bgee; ENSSSCG00000016613; Expressed in liver and 42 other cell types or tissues.
DR   ExpressionAtlas; A0A287B8T1; baseline and differential.
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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 3.
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   1: Evidence at protein level;
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A287B8T1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT   DOMAIN          27..157
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01003"
FT   DOMAIN          197..399
FT                   /note="Alanine dehydrogenase/pyridine nucleotide
FT                   transhydrogenase NAD(H)-binding"
FT                   /evidence="ECO:0000259|SMART:SM01002"
SQ   SEQUENCE   823 AA;  91561 MW;  020C472617BD7BF3 CRC64;
     MLRLSRPKLG RLRLSLSKRL HHKAVMALRR EDVNAWERRA PLAPRHVKGI TNLGYKVLIQ
     PSNRRAIHDK EYVKAGGILQ EDISEACLIL GVKRPPEEKL MSKKTYAFFS HTIKAQEANM
     GLLDEILKQE IRLIDYEKMV DHRGIRVVAF GQWAGVAGML NILHGMGLRL LALGHHTPFM
     HIGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQEIFNELPC
     EYVEPHELKE VSQTGDLRKV YGTVLSRHHH LVRKTDGVYD PIEYDKHPER YTSRFSTDIA
     PYTTCLINGI YWEQNTPRLL TRQDAQSLLA PGKSSVAGVE GCPALPHKLV AICDISADTG
     GSIEFMTECT TIEHPFCMYD ADQHIIHDSV EGSGILMCSI DNLPAQLPIE STEYFGDMLY
     PFVEEMILSD ATQPLESQNF SPVVRDAVIT SNGTLAKKYK YIQTLRESRE RAQSLSMGTK
     KKVLVLGSGY VSEPVLEYLS RDDNVEITVG SDMKNQIEQL GKKYGINPVS LDVGKQEEKL
     GSLVATQDLV ISLLPYVLHP LVAKACIASK VNMITASYIT PALKELEKSV EDAGITVIGE
     LGLDPGLDHM LAMETIDKAK EVGATIESYT SYCGGLPAPE HSNNPLRYKF SWSPVGVLMN
     IMQPATYLLN GKVVNVVGGV SFLDSVTPMD YFPGLNLEGY PNRDSTKYAE IYGISSAHTL
     LRGTLRYKGY AKALNGFVKL GLINRDVFPA LQPEASPLTW KELLCDLVGI LPSSKSDVLK
     EAVFKKLGGD SAQLEAAEWP WRERYDCDER QLWNQTSFWT SRK
//