ID G3S008_GORGO Unreviewed; 892 AA.
AC G3S008;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Aminoadipate-semialdehyde synthase {ECO:0000313|Ensembl:ENSGGOP00000021401.2};
GN Name=AASS {ECO:0000313|Ensembl:ENSGGOP00000021401.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000021401.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000021401.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000021401.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000021401.2}
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; CABD030054795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030054796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3S008; -.
DR STRING; 9593.ENSGGOP00000021401; -.
DR Ensembl; ENSGGOT00000034197.2; ENSGGOP00000021401.2; ENSGGOG00000027257.2.
DR GeneTree; ENSGT00390000013249; -.
DR HOGENOM; CLU_005231_0_1_1; -.
DR InParanoid; G3S008; -.
DR OMA; TPHVHDI; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000001519; Chromosome 7.
DR Bgee; ENSGGOG00000027257; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
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:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
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:UP000001519}.
FT DOMAIN 27..137
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 178..380
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 892 AA; 98640 MW; 5D1EC446EAD934DC CRC64;
MLQVHRTGLG RLGVSLSKGL HHKAVLAVRR EDVNAWERRA PLAPKHIKGI TNLGYKVLIQ
PSNRRAIHDK DYVKAGGILQ EDISEACLIL GVKRPPEEKL MSRKTYAFFS HTIKAQEANM
GLLDEILKQS FYWSDSVTGM INILHGMGLR LLALGHHTPF MHIGMAHNYR NSSQAVQAVR
DAGYEISLGL MPKSIGPLTF VFTGTGNVSK GAQAIFNELP CEYVEPHELK EVSQTGDLRK
VYGTVLSRHH HLVRKTDRVY DPAEYDKHPE RYISRFNTDI APYTTCLING IYWEQNTPRL
LTRQDAQSLL APGKFSAAGV EGCPALPHKL VAICDISADT GGSIEFMTEC TTIERPFCMY
DADQHIIHDS VEGSGILMCS IDNLPAQLPI EATECFGDML YPYVEEMILS DATQPLESQN
FSPVVRDAVI TSNGTLPDKY KYIQTLRESR ERAQSLSMGT RRKVLVLGSG YVSEPVLEYL
SRDDVKIYFT LTYLKIMDIC KQEEKLGFLV AKQDLVISLL PYVLHPLVAK ACITNKVNMV
TASYITPALK ELEKSVEDAG ITIIGELGLD PGLDHMLAME TIDKAKEVGA TIESYISYCG
GLPAPEHSNN PLRYKFSWSP VGVLMNVMQS ATYLLDGKVV NVAGGISFLD AVTSMDFFPG
LNLEGYPNRD STKYAEIYGI SSAHTLLRGT LRYKGYMKAL NGFVKLGLIN REALPAFRPE
ANPLTWKQLL CDLVGISPSS EHNVLKEAVL KRLGGDNTQL EAAEWLGLLG DEQVPQAESI
LDALSKHLVM KLSYGPEEKD MIVMRDSFGI RHPSGHLEHK TIDLVAYGNI NGFSAMAKTV
GLPTAMAAKM LLDGEIGSKG LMGPFSKEIY GPILERIKAE GIIYTTQSTI KP
//
