AASS_BOVIN
ID AASS_BOVIN Reviewed; 926 AA.
AC A8E657;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Alpha-aminoadipic semialdehyde synthase, mitochondrial {ECO:0000250|UniProtKB:Q9UDR5};
DE AltName: Full=LKR/SDH {ECO:0000250|UniProtKB:Q9UDR5};
DE Includes:
DE RecName: Full=Lysine ketoglutarate reductase {ECO:0000250|UniProtKB:Q9UDR5};
DE Short=LKR {ECO:0000250|UniProtKB:Q9UDR5};
DE Short=LOR;
DE EC=1.5.1.8 {ECO:0000250|UniProtKB:Q9UDR5};
DE Includes:
DE RecName: Full=Saccharopine dehydrogenase {ECO:0000250|UniProtKB:Q9UDR5};
DE Short=SDH {ECO:0000250|UniProtKB:Q9UDR5};
DE EC=1.5.1.9 {ECO:0000250|UniProtKB:Q9UDR5};
DE Flags: Precursor;
GN Name=AASS {ECO:0000250|UniProtKB:Q9UDR5};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1] {ECO:0000312|EMBL:AAI53852.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI53852.1};
RC TISSUE=Uterus {ECO:0000312|EMBL:AAI53852.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the first two steps in
CC lysine degradation. {ECO:0000250|UniProtKB:Q9UDR5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + NADP(+) = 2-oxoglutarate + H(+) + L-
CC lysine + NADPH; Xref=Rhea:RHEA:19373, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57951, ChEBI:CHEBI:58349; EC=1.5.1.8;
CC Evidence={ECO:0000250|UniProtKB:Q9UDR5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:19375;
CC Evidence={ECO:0000250|UniProtKB:Q9UDR5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + NAD(+) = (S)-2-amino-6-oxohexanoate +
CC H(+) + L-glutamate + NADH; Xref=Rhea:RHEA:24520, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57951, ChEBI:CHEBI:58321; EC=1.5.1.9;
CC Evidence={ECO:0000250|UniProtKB:Q9UDR5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24521;
CC Evidence={ECO:0000250|UniProtKB:Q9UDR5};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC {ECO:0000250|UniProtKB:Q9UDR5}.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC {ECO:0000250|UniProtKB:Q9UDR5}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q99K67}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9UDR5}.
CC -!- DOMAIN: The N-terminal and the C-terminal domains contain respectively
CC the lysine ketoglutarate reductase and saccharopine dehydrogenase
CC activity. {ECO:0000250|UniProtKB:Q9UDR5}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000255}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000255}.
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DR EMBL; BC153851; AAI53852.1; -; mRNA.
DR RefSeq; NP_001103267.1; NM_001109797.1.
DR AlphaFoldDB; A8E657; -.
DR SMR; A8E657; -.
DR STRING; 9913.ENSBTAP00000016090; -.
DR PaxDb; A8E657; -.
DR PeptideAtlas; A8E657; -.
DR PRIDE; A8E657; -.
DR Ensembl; ENSBTAT00000016090; ENSBTAP00000016090; ENSBTAG00000012128.
DR Ensembl; ENSBTAT00000080443; ENSBTAP00000058471; ENSBTAG00000012128.
DR GeneID; 520865; -.
DR KEGG; bta:520865; -.
DR CTD; 10157; -.
DR VEuPathDB; HostDB:ENSBTAG00000012128; -.
DR VGNC; VGNC:25451; AASS.
DR eggNOG; KOG0172; Eukaryota.
DR GeneTree; ENSGT00390000013249; -.
DR InParanoid; A8E657; -.
DR OMA; KMEGRSE; -.
DR OrthoDB; 498994at2759; -.
DR UniPathway; UPA00868; UER00835.
DR UniPathway; UPA00868; UER00836.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000012128; Expressed in adult mammalian kidney and 114 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; ISS:UniProtKB.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; ISS:UniProtKB.
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 GO; GO:0006554; P:lysine catabolic process; ISS:UniProtKB.
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 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; SSF51735; SSF51735; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Mitochondrion; Multifunctional enzyme; NAD; NADP;
KW Oxidoreductase; Reference proteome; Transit peptide.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 28..926
FT /note="Alpha-aminoadipic semialdehyde synthase,
FT mitochondrial"
FT /id="PRO_0000315867"
FT REGION 28..455
FT /note="Lysine-ketoglutarate reductase"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT REGION 477..926
FT /note="Saccharopine dehydrogenase"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT BINDING 488
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UDR5"
FT BINDING 512
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UDR5"
FT BINDING 516
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UDR5"
FT BINDING 554
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UDR5"
FT BINDING 576
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UDR5"
FT BINDING 577..578
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 577
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UDR5"
FT BINDING 603
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UDR5"
FT BINDING 604
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 604
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UDR5"
FT BINDING 605
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q9UDR5"
FT BINDING 703
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 724..726
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 93
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 93
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 138
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 138
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 274
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 286
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 286
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 333
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 458
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 458
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 523
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 523
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 535
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 535
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 584
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 584
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 707
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 732
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 739
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 761
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 761
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
FT MOD_RES 780
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99K67"
SQ SEQUENCE 926 AA; 102084 MW; 81A826B1856D9604 CRC64;
MLRVSRTKLG RLSPSLSRGL HHKAVMALRR EDVNAWERRA PLAPRHVKGI TNLGYKVLIQ
PSNRRAIHDK EYVKAGGILQ EDISEACLIL GVKRPPEEKL MPKKTYAFFS HTIKAQEANM
GLLDEILKQE IRLIDYEKMV DHRGIRVVAF GQWAGVAGII NILHGMGLRL LALGHHTPFM
HIGMAHNYRN SGQAVQAVRD AGYEISLGLM PKSIGPLTFV FTGTGNVSKG AQEIFNELPC
EYVEPHELKE VSQNGDLRKV YGTVLSRHHH LVRKTDGVYD PVEYDKYPER YISRFNTDIA
PYTTCLINGI YWEQNTPRLL TRQDAQSLLA PGKSPVAGVE GCPALPHKLV AICDISADTG
GSIEFMTECT TIERPFCMYD ADQHIIHDSV EGSGILMCSI DNLPAQLPIE STEYFGDMLY
PYVEEMILSD ATQPLESQNF SPVVRDAVIA SNGMLSNKYK YIQKLRENRE HAQSLSMGTK
KKVLVLGSGY VSEPVLEYLL RDDSIEITVG SDMKNQIEQL GKKYNINPVS LHVGKQEEKL
SSLVATQDLV ISLLPYVLHP LVAKACIASK VNMITASYIT PALKELEKSV EDAGITVIGE
LGLDPGLDHM LAMETIDKAK EVGATIESYV SYCGGLPAPE CSDNPLRYKF SWSPVGVLMN
IMQPATYLLN GKVVNAVGGV SFLDSVTPMD YFPGLNLEGY PNRDSTKYAE IYGIPSAHTL
LRGTLRYKGY AKALSGFVKL GLINRDAFPA LQPDANPLTW KELLCDLVGI SSSSKCDVLK
EAVFKKLGGD TTQLEALEWL GLLGDEQVPQ AESLVDALSK HLAVKLSYGP GEKDMIVMRD
SFGIRHPSGH LENKTIDLVV YGDVNGFSAM AKTVGLPTAM AAKMLLDGEI QAKGLMGPFS
KEIYGPILER IKAEGIMYTT QSTIKL
