ID   AL7A1_CTEID             Reviewed;          21 AA.
AC   P84463;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 39.
DE   RecName: Full=Alpha-aminoadipic semialdehyde dehydrogenase;
DE            Short=Alpha-AASA dehydrogenase;
DE            EC=1.2.1.31;
DE   AltName: Full=Aldehyde dehydrogenase family 7 member A1;
DE   AltName: Full=Antiquitin-1;
DE   AltName: Full=Delta1-piperideine-6-carboxylate dehydrogenase;
DE            Short=P6c dehydrogenase;
DE   Flags: Fragment;
GN   Name=aldh7a1;
OS   Ctenopharyngodon idella (Grass carp) (Leuciscus idella).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Xenocyprididae; Xenocypridinae; Ctenopharyngodon.
OX   NCBI_TaxID=7959;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBUNIT.
RC   TISSUE=Liver {ECO:0000269|PubMed:14602152};
RX   PubMed=14602152; DOI=10.1016/s1096-4959(03)00248-3;
RA   Chan W.-M., Tang W.-K., Cheng C.H., Fong W.-P.;
RT   "Purification, N-terminal sequence determination and enzymatic
RT   characterization of antiquitin from the liver of grass carp.";
RL   Comp. Biochem. Physiol. 136B:443-450(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-amino-6-oxohexanoate + H2O + NADP(+) = 2 H(+) + L-2-
CC         aminoadipate + NADPH; Xref=Rhea:RHEA:12304, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58321,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58672; EC=1.2.1.31;
CC         Evidence={ECO:0000269|PubMed:14602152};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-2-amino-6-oxohexanoate + H2O + NAD(+) = 2 H(+) + L-2-
CC         aminoadipate + NADH; Xref=Rhea:RHEA:12308, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58321, ChEBI:CHEBI:58672; EC=1.2.1.31;
CC         Evidence={ECO:0000269|PubMed:14602152};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.0 mM for acetaldehyde {ECO:0000269|PubMed:14602152};
CC         Vmax=1.95 umol/min/mg enzyme {ECO:0000269|PubMed:14602152};
CC       pH dependence:
CC         Optimum pH is 9-10. {ECO:0000269|PubMed:14602152};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:14602152}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P84463; -.
DR   SABIO-RK; P84463; -.
DR   GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..>21
FT                   /note="Alpha-aminoadipic semialdehyde dehydrogenase"
FT                   /id="PRO_0000056494"
FT   NON_TER         21
FT                   /evidence="ECO:0000303|PubMed:14602152"
SQ   SEQUENCE   21 AA;  2289 MW;  A69E54BB27B2EF1A CRC64;
     SALAINQPNY SVLKELGLNE D