ID H3AAU5_LATCH Unreviewed; 935 AA.
AC H3AAU5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Aminoadipate-semialdehyde synthase {ECO:0000313|Ensembl:ENSLACP00000006766.1};
GN Name=AASS {ECO:0000313|Ensembl:ENSLACP00000006766.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000006766.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000006766.1}
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; AFYH01231350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01231351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01231352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01231353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01231354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01231355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01231356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01231357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006011556.1; XM_006011494.2.
DR AlphaFoldDB; H3AAU5; -.
DR STRING; 7897.ENSLACP00000006766; -.
DR Ensembl; ENSLACT00000006822.1; ENSLACP00000006766.1; ENSLACG00000006003.1.
DR GeneID; 102353181; -.
DR KEGG; lcm:102353181; -.
DR CTD; 10157; -.
DR eggNOG; KOG0172; Eukaryota.
DR GeneTree; ENSGT00390000013249; -.
DR HOGENOM; CLU_005231_0_1_1; -.
DR InParanoid; H3AAU5; -.
DR OMA; TPHVHDI; -.
DR OrthoDB; 2184985at2759; -.
DR TreeFam; TF105728; -.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000006003; Expressed in muscle tissue and 2 other cell types or tissues.
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:UP000008672}.
FT DOMAIN 33..163
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 203..405
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 935 AA; 103882 MW; E1198E2BF9F00550 CRC64;
MKFGLAMLRL LMHKSREFGL CHARCNYHKA VLAIRREDIN AWERRAPLAP RHVKELTNEG
YKVLVQPSNR RAIHEKDYIK AGAIIQEDIS EASIIIGVKR PPEEKLIPKK TYACFSHTIK
AQEANMGLLD DILKKEVRLI DYEKMVDQKG MRVVAFGQWA GVAGMINILH GLGLRFLALG
HHTPFMHIGM AHNYRNSSQA VQAVRDAGYE ISLGLMPKSI GPLTFVFTGS GNVSKGAQEI
FNELPCEFVE SHELREVSQS GDLRKVYGTV LSRHHHLVRK NNGKYDPGDY DQYPELYTSR
FNTDIAPYTT CLINGIYWDP QTPRLLNRQD AQRLLAPCKP SPDSYEGCPL LPHKFLAICD
ISADTGGSIE FMTECTTIDV PFCMYDADQH IIHDSVEGNG ILMCSIDNLP AQLPIEATEY
FGDRLFPYIW EMLSSNATVP FEEQEGFSSV IRDAVIASNG KLTPKYTYIQ KLRENREREA
FQALKMSKKK VLLLGSGYVS GPVLDYLSRD PNIELTVASV MKQQMEQLAK KYRNTTPVVL
DVIKEEDVLS SLVKEHDLVI SLLPNVFHPH VAKQCISSKV NLVTASYLLP AMKELQKSAE
DAGITVVNEV GLDPGIDHML AMECFDDAKE KGAKVESYIS FCGGLPAPEC SENPLRYKFS
WSPRGVLLNT IGAATFLKNG QVTNIPAGGA LLDSTMTMNF LPGFSLEGFP NRDSTKYVEL
YGIQSAHTLL RGTLRFKGFS ATVNGFIKLG MINTEPCDLL SSNAPPITWR ALLSRLIGVS
PSASLDSLKD AIYNKLERDD DRLKALMWLG LLSDEVVPKA ESILDALAKH LENKLAFSHG
ERDMIIMRSD IGIRHPSGHL ETKHISLVLY GDPAGFSAMA KAVGYPTAIA AKIVLDGEIT
TKGMILPLTK DFYGPMLERI KAEGIMYTTG STLSS
//
