AL8A1_BOVIN
ID AL8A1_BOVIN Reviewed; 487 AA.
AC Q0P5F9; A1L594;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) 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; BT029881; ABM06132.1; -; mRNA.
DR EMBL; BC120092; AAI20093.1; -; mRNA.
DR RefSeq; NP_001069094.1; NM_001075626.1.
DR AlphaFoldDB; Q0P5F9; -.
DR SMR; Q0P5F9; -.
DR STRING; 9913.ENSBTAP00000010485; -.
DR PaxDb; Q0P5F9; -.
DR PeptideAtlas; Q0P5F9; -.
DR PRIDE; Q0P5F9; -.
DR GeneID; 513537; -.
DR KEGG; bta:513537; -.
DR CTD; 64577; -.
DR eggNOG; KOG2450; Eukaryota.
DR HOGENOM; CLU_005391_0_0_1; -.
DR InParanoid; Q0P5F9; -.
DR OrthoDB; 899961at2759; -.
DR TreeFam; TF314129; -.
DR UniPathway; UPA00334; -.
DR Proteomes; UP000009136; Unplaced.
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; ISS:UniProtKB.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042574; P:retinal metabolic process; ISS:UniProtKB.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISS:UniProtKB.
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_0000312953"
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"
FT CONFLICT 47
FT /note="I -> V (in Ref. 1; ABM06132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 487 AA; 53363 MW; 3EC8B8DAB4AE5414 CRC64;
MAGRGGLLML ENFIGGKFLP CSSYLDSYDP STGEVYCHVP NSGKEEIEAA VEAARAAFPG
WSSRSPQERS QVLQRLADLL EQSLEELAQA ESKDQGKTIT LARTMDIPRA VHNFRFFASS
ILHHTSECTQ MDHLGCLHYT VRAPVGIAAL ISPWNLPLYL LTWKIAPAIA AGNTVIAKPS
ELTSVTAWMM CRLLEKAGVP PGVVNIVFGT GPRVGEALVS HPEVPLISFT GSQPTAERIM
QLSAPHCKKL SLELGGKNPA VIFEDANLAE CIPTTVRSSF ANQGEICLCT SRIFVQRSIY
SEFLKRFVEA ARMWKVGIPS DPSADMGALI SKAHLEKVRS YIKKARMEGA QILCGEGVDK
LNLPPRNQAG YFMLPTVITD VKDESCCMKE EIFGPVTCVV PFDSEEEVIQ RANNVKYGLA
ATVWSGNVGR VHRVAKKLQS GLVWTNCWLI RELNLPFGGM KSSGVGREGA KDSYEFFTEV
KTITVKH
