ID A0A2I3H6G7_NOMLE Unreviewed; 917 AA.
AC A0A2I3H6G7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Aminoadipate-semialdehyde synthase {ECO:0000313|Ensembl:ENSNLEP00000039199.1};
GN Name=AASS {ECO:0000313|Ensembl:ENSNLEP00000039199.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000039199.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000039199.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000039199.1}
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 EMBL; ADFV01195804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01195805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01195806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01195807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01195808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3H6G7; -.
DR Ensembl; ENSNLET00000034914.1; ENSNLEP00000039199.1; ENSNLEG00000011978.2.
DR GeneTree; ENSGT00390000013249; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000001073; Chromosome 13.
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; 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 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:UP000001073}.
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 917 AA; 101316 MW; 63BDCA1B8C744EFC CRC64;
MLQVHRTGLG RLGVSLSKGL HHKAVLAVRR EDVNAWERRA PLAPKHIKGI TNLGYKVLIQ
PSNRRAIHDK DYVKAGGILQ EDISEACLIL GVKRPPEEKL MSRKTYAFFS HTIKAQEANM
GLLDEILKQE IRLIDYEKMV DHRGVRVVAF GQWAGVAGMI NILHGMGLRL LALGHHTPFM
HIGMAHNYRN SSQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQAIFNELPC
EYVEPHELKE VSQTGDLRKV YGTVLSRHHH LVRKTDGVYD PAEYDKHPER YISRFNTDIA
PYTTCLINGI YWEQNTPRLL TRQDAQSLLA PGKFSAAGVE GCPALPHKLV AICDISADTG
GSIEFMTECT TIERPFCMYD ADQHIIHDSV EGSGILMCSI DNLPAQLPIE ATECFGDMLY
PYVEEMILSD ATQPLESQNF SPVVRDAVIT SNGTLPDKYK YIQTLRESRE RAQSLSMGTR
RKVLVLGSGY VSEPHVDFYI LKDYFNQIEQ LGKKYNINPV SMDICKQEEK LGFLVAKQDL
VISLLPYVLH PLVAKACITN KVNMVTASYI TPALKELEKS VEDAGITIIG ELGLDPGLDH
MLAMETIDKA KEVGATIESY ISYCGGLPAP EHSNNPLRYK FSWSPVGVLM NVMQSATYLL
NGKVVNVAGG ISFLDAVTSM DFFPGLNLEG YPNRDSTKYA EIYGISSAHT LLRGTLRYKG
YMKALNGFVK LGLINREALP AFRPEANPLT WKQLLCDLVG ISPSSEHDVL KEAVLKKLGG
DNTQLEAAEW LGLLGDEQVP QAESILDALS KHLVMKLSYG PEEKDMIVMR DSFGIRHPSG
HLEHKTIDLV AYGDINGFSA MAKTVGLPTA MAAKMLLDGE IGAKGLMGPF SKEIYGPILE
RIKAEGIIYT TQSTIKP
//
