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
//