ID A0A151PFJ0_ALLMI Unreviewed; 944 AA.
AC A0A151PFJ0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Alpha-aminoadipic semialdehyde synthase, mitochondrial {ECO:0000313|EMBL:KYO47545.1};
GN Name=AASS {ECO:0000313|EMBL:KYO47545.1};
GN ORFNames=Y1Q_0019666 {ECO:0000313|EMBL:KYO47545.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO47545.1};
RN [1] {ECO:0000313|EMBL:KYO47545.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO47545.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO47545.1}.
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DR EMBL; AKHW03000416; KYO47545.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151PFJ0; -.
DR STRING; 8496.A0A151PFJ0; -.
DR eggNOG; KOG0172; Eukaryota.
DR UniPathway; UPA00868; UER00835.
DR Proteomes; UP000050525; Unassembled WGS sequence.
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:UP000050525}.
FT DOMAIN 44..174
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase N-terminal"
FT /evidence="ECO:0000259|SMART:SM01003"
FT DOMAIN 214..416
FT /note="Alanine dehydrogenase/pyridine nucleotide
FT transhydrogenase NAD(H)-binding"
FT /evidence="ECO:0000259|SMART:SM01002"
SQ SEQUENCE 944 AA; 104785 MW; 65A5B5EFDBC0E7C3 CRC64;
MLCCITTLSL QLSGFIMLRA FRHTNGKFGH HHLQSRDHHK SVLAIRREDV NVWERRAPLA
PKHIKELTRL GYKVLVQPSN RRAIHEKDYV KAGGIIQEDI SKASLIVGVK RPPEDKLIPK
KTYAFFSHTI KAQEANMSLL DEILRQEIRL IDYEKMVDHR GVRVVAFGKW AGVAGMINIL
HGMGLRFLAL GHHTPFMHIG MAHNYRNSNQ AVQAVRDAGY EISLGLMPKS LGPLTFVFTG
TGNVSKGAQE MFNALPCEFV EPHELKEVSK SGDLRKVYGT VLSRHHHLVR KSDGVYDPAE
YEKHPELYTS RFNTNIAPYT TCLINGIYWE QDTPRLLSRQ DAQRLLVPHK SPSLAIEGCP
ELPHKLLAIC DISADTGGSI EFMTECTTIN NPFCIYDADQ HIIHDSVEGF GILMCSIDNL
PAQLPIESTE YFGDMLFPYI EEMLLSEGSE PLESQNYSPV VRDAVIASNG SLTPKYKYIQ
KLRESREYAQ SLTMDKKKKV LLLGAGYVSG PVIEYLTRDP NIQITAASFM KEQLEQLTKK
HSNVTSVIMD VIKHEDKLST LVKKHDLVIS LLPYSAHPLV AKKCIDSKVN LVTASYLTPA
MKELQESVEA AGITVISEMG LDPGLDHMLA MECIDKAKEV GATVVSYTSF CGGLPAPEYS
DNPLRYKFSW SPQGVLLNTV QPAVYLKNGE VINIPAGGAL LDSVIPMDFF PGLNLEGFPN
RDSTKYAEPY GIQSAHTLLR GTLRYKGYSK AMGGFVKLGL VNSDPYPLVS ATAPSITWKG
LMCQLLGLKP SVKSSSLKEA VYNKLGKDNS QLEAVEWLGL LGDEPVPIAD SIVGALAKHM
ERKLPFGAGE RDMIVMRNEI GLRHPSGHFE DKLIDLVVYG DDKGYSAMAK TVGYPTAIAA
KMVLNGEIDA KGMVIPLTKN IYGPVLERIR SEGIVYRTQS VIRQ
//
