ID   AL8A1_DANRE             Reviewed;         487 AA.
AC   Q66I21;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=2-aminomuconic semialdehyde dehydrogenase;
DE            EC=1.2.1.32 {ECO:0000250|UniProtKB:Q9H2A2};
DE   AltName: Full=Aldehyde dehydrogenase family 8 member A1;
GN   Name=aldh8a1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Intestine;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD-dependent oxidation of 2-aminomuconic
CC       semialdehyde of the kynurenine metabolic pathway in L-tryptophan
CC       degradation. {ECO:0000250|UniProtKB:Q9H2A2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-aminomuconate 6-semialdehyde + H2O + NAD(+) = (2Z,4E)-2-
CC         aminomuconate + 2 H(+) + NADH; Xref=Rhea:RHEA:14469,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:77634, ChEBI:CHEBI:77859; EC=1.2.1.32;
CC         Evidence={ECO:0000250|UniProtKB:Q9H2A2};
CC   -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation.
CC       {ECO:0000250|UniProtKB:Q9H2A2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; BC081581; AAH81581.1; -; mRNA.
DR   EMBL; BC152164; AAI52165.1; -; mRNA.
DR   RefSeq; NP_001004540.1; NM_001004540.1.
DR   AlphaFoldDB; Q66I21; -.
DR   SMR; Q66I21; -.
DR   STRING; 7955.ENSDARP00000053398; -.
DR   PaxDb; Q66I21; -.
DR   Ensembl; ENSDART00000053399; ENSDARP00000053398; ENSDARG00000036776.
DR   GeneID; 447801; -.
DR   KEGG; dre:447801; -.
DR   CTD; 64577; -.
DR   ZFIN; ZDB-GENE-040912-3; aldh8a1.
DR   eggNOG; KOG2450; Eukaryota.
DR   GeneTree; ENSGT00940000156799; -.
DR   HOGENOM; CLU_005391_0_2_1; -.
DR   InParanoid; Q66I21; -.
DR   OMA; PMPIAAW; -.
DR   OrthoDB; 899961at2759; -.
DR   PhylomeDB; Q66I21; -.
DR   TreeFam; TF314129; -.
DR   Reactome; R-DRE-5365859; RA biosynthesis pathway.
DR   UniPathway; UPA00334; -.
DR   PRO; PR:Q66I21; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 23.
DR   Bgee; ENSDARG00000036776; Expressed in liver and 19 other tissues.
DR   ExpressionAtlas; Q66I21; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047102; F:aminomuconate-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR   GO; GO:0001758; F:retinal dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001889; P:liver development; IMP:ZFIN.
DR   GO; GO:0042573; P:retinoic acid metabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN           1..487
FT                   /note="2-aminomuconic semialdehyde dehydrogenase"
FT                   /id="PRO_0000312956"
FT   ACT_SITE        253
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        287
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         231..236
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            155
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   487 AA;  53354 MW;  4F13284B613DE146 CRC64;
     MSKDMKYLVL ENYIGGKFVP CSKLIDSFDP STGEVYCKVP DSGAEEVNAA VRAAKEAFPD
     WSAKSPADRS KVLNKLADLI EARLEEFVQA ESKDQGKTIT FARNVDIPRS AYNFRFFASS
     VLHHTNDCSQ MDHMGCLNYT IRCPVGVAGL ISPWNLPLYL LTWKIAPAVA TGNTVVAKPS
     EMTSVTAWMM CQLLEEAGFP PGVVNIVFGT GPRAGDALVS HPDVPLISFT GSTATARLIT
     ERSAPHCKKL SLELGGKNPA IIFADADMEQ CISTTVRSSF SNQGEICLCT SRIFVERSVY
     PEFLTRFVEA TRRWKTGVPS DPSNDNGALI SKEHLQKVKG YITLALAEGA QVHCGEGVDK
     LALPQQNIGG YFMLPTIISG VKDSSALMQE EIFGPVTCVT PFDEEEEVIS RANNVRYGLS
     ATVWSRDVGR VHRVARKLQA GLVWTNCWLV RDLNLPFGGM KHSGIGREGG KDSYHFFTEV
     KSVTVKH