ID   AL7A1_ACASC             Reviewed;          18 AA.
AC   P83402;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 54.
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   Acanthopagrus schlegelii (Black porgy).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Acanthopagrus.
OX   NCBI_TaxID=72011 {ECO:0000305};
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   TISSUE=Liver;
RX   PubMed=11959129; DOI=10.1016/s0014-5793(02)02553-x;
RA   Tang W.-K., Cheng C.H.K., Fong W.-P.;
RT   "First purification of the antiquitin protein and demonstration of its
RT   enzymatic activity.";
RL   FEBS Lett. 516:183-186(2002).
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:11959129};
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:11959129};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.0 mM for acetaldehyde;
CC         Vmax=1.3 umol/min/mg enzyme;
CC       pH dependence:
CC         Optimum pH is 9-10.;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11959129}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   AlphaFoldDB; P83402; -.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR   GO; GO:0004043; F:L-aminoadipate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase.
FT   CHAIN           1..>18
FT                   /note="Alpha-aminoadipic semialdehyde dehydrogenase"
FT                   /id="PRO_0000056493"
FT   NON_TER         18
FT                   /evidence="ECO:0000303|PubMed:11959129"
SQ   SEQUENCE   18 AA;  2059 MW;  BFF8C3EF1A9B4047 CRC64;
     SGLLINQPKY SWLKELGL