ID A0A2Y9T112_PHYMC Unreviewed; 925 AA.
AC A0A2Y9T112;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Alpha-aminoadipic semialdehyde synthase, mitochondrial isoform X1 {ECO:0000313|RefSeq:XP_023984053.1};
GN Name=AASS {ECO:0000313|RefSeq:XP_023984053.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_023984053.1};
RN [1] {ECO:0000313|RefSeq:XP_023984053.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_023984053.1};
RG RefSeq;
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 RefSeq; XP_023984053.1; XM_024128285.3.
DR AlphaFoldDB; A0A2Y9T112; -.
DR STRING; 9755.ENSPCTP00005004359; -.
DR Ensembl; ENSPCTT00005004812; ENSPCTP00005004359; ENSPCTG00005003140.
DR KEGG; pcad:102992598; -.
DR InParanoid; A0A2Y9T112; -.
DR OrthoDB; 2184985at2759; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000248484; Chromosome 5.
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: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:UP000248484}.
FT DOMAIN 26..156
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 196..398
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 925 AA; 102314 MW; FFFF058F5424906B CRC64;
MLRVPRTKLG GLGLSLSRLH YKAVMALRRE DVNAWERRAP LAPRHIKGIT NLGYKVLIQP
SNRRAIHDKE YVKAGGILQE DISEACLILG VKRPPEEKLM PKKTYAFFSH TIKAQEANMG
LLDEILKQEI RLIDYEKMVD HRGIRVVAFG QWAGVAGMIN ILHGMGLRLL ALGHHTPFMH
IGMAHNYRNS SQAVQAVRDT GYEISLGLMP KSIGPLTFVF TGTGNVSKGA QEIFNELPCE
YVEPHELKEV SQNGDLRKVY GTVLSRHHHL VRKTDGIYDP VEYDKYPERY ISRFNTDIAP
YTTCLINGIY WEQNTPRLLT RQDAQSLLAP GKSSVAGVEG CPALPHKLVA LCDISADTGG
SIEFMTECTT IEHPFCMYDA DQHIIHDSVE GSGILMCSID NLPAQLPIES TEYFGDMLYP
YVEEMILSDA TQPLESQNFS PVVRDAVITS NGTLSNKYKY IQKLRESRER VQSLSVGTKK
KVLVLGSGYV SEPVLEYLSR DDNIEITVGS DMKNQIEQLG KKYNINPVSL YVGKQEVKLS
SLVATQDLVI SLLPYVLHPL VAKACIASKV NMITASYITP VLKELEKSME DAGITVIGEL
GLDPGLDHML AMETIDKAKE VGATIESYVS YCGGLPAPEH SDNPLRYKFS WSPVGVLMNI
MQPATYLLNG KVVNVVGGVS FLDSVTPMDY FPGLNLESYP NRDSTRYAGI YGIPSAHTLL
RGTLRYKGYA KALNGFVKLG LINRDAFPAL RPDANPLTWK ELLCDLVGIS PSSKCDVLKE
AVFKKLEGDN TQLEAVEWLG LLGDEQVPRA ESLVDALSKH LAMKLSYGPG EKDMIVMRDN
FGIRHPSGHL EKKTIDLVVY GDVNGFSAMA KTVGLPTAMA AKMLLDGEIQ AKGLMGPFSK
EIYGPILERI KAEGIMYTTQ STITP
//
