AL1A1_CHICK
ID AL1A1_CHICK Reviewed; 509 AA.
AC P27463;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Aldehyde dehydrogenase 1A1 {ECO:0000250|UniProtKB:P00352};
DE EC=1.2.1.19 {ECO:0000250|UniProtKB:P24549};
DE EC=1.2.1.28 {ECO:0000250|UniProtKB:P00352};
DE EC=1.2.1.3 {ECO:0000250|UniProtKB:P00352};
DE EC=1.2.1.36 {ECO:0000250|UniProtKB:P51647};
DE AltName: Full=3-deoxyglucosone dehydrogenase {ECO:0000250|UniProtKB:P00352};
DE AltName: Full=ALDH-E1;
DE AltName: Full=ALHDII;
DE AltName: Full=Aldehyde dehydrogenase family 1 member A1;
DE AltName: Full=Aldehyde dehydrogenase, cytosolic {ECO:0000305|PubMed:1559558};
DE AltName: Full=Retinal dehydrogenase 1 {ECO:0000305};
DE Short=RALDH 1 {ECO:0000305};
DE Short=RalDH1 {ECO:0000305};
GN Name=ALDH1A1 {ECO:0000250|UniProtKB:P00352};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic retina;
RX PubMed=1559558; DOI=10.1016/s0014-4835(05)80219-2;
RA Godbout R.;
RT "High levels of aldehyde dehydrogenase transcripts in the undifferentiated
RT chick retina.";
RL Exp. Eye Res. 54:297-305(1992).
CC -!- FUNCTION: Cytosolic dehydrogenase that catalyzes the irreversible
CC oxidation of a wide range of aldehydes to their corresponding
CC carboxylic acid (By similarity). Functions downstream of retinol
CC dehydrogenases and catalyzes the oxidation of retinaldehyde into
CC retinoic acid, the second step in the oxidation of retinol/vitamin A
CC into retinoic acid. This pathway is crucial to control the levels of
CC retinol and retinoic acid, two important molecules which excess can be
CC teratogenic and cytotoxic (By similarity). Also oxidizes aldehydes
CC resulting from lipid peroxidation like (E)-4-hydroxynon-2-enal/HNE,
CC malonaldehyde and hexanal that form protein adducts and are highly
CC cytotoxic. By participating for instance to the clearance of (E)-4-
CC hydroxynon-2-enal/HNE in the lens epithelium prevents the formation of
CC HNE-protein adducts and lens opacification. Functions also downstream
CC of fructosamine-3-kinase in the fructosamine degradation pathway by
CC catalyzing the oxidation of 3-deoxyglucosone, the carbohydrate product
CC of fructosamine 3-phosphate decomposition, which is itself a potent
CC glycating agent that may react with lysine and arginine side-chains of
CC proteins (By similarity). Has also an aminobutyraldehyde dehydrogenase
CC activity and is probably part of an alternative pathway for the
CC biosynthesis of GABA/4-aminobutanoate in midbrain, thereby playing a
CC role in GABAergic synaptic transmission (By similarity).
CC {ECO:0000250|UniProtKB:P00352, ECO:0000250|UniProtKB:P24549}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16186;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2
CC H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-cis-retinal + H2O + NAD(+) = 9-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:42084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78273,
CC ChEBI:CHEBI:78630; Evidence={ECO:0000250|UniProtKB:P51647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42085;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=11-cis-retinal + H2O + NAD(+) = 11-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:47132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16066, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:87435; Evidence={ECO:0000250|UniProtKB:P51647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47133;
CC Evidence={ECO:0000250|UniProtKB:P51647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-retinal + H2O + NAD(+) = 13-cis-retinoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:67332, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:45487, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:169952; Evidence={ECO:0000250|UniProtKB:Q8HYE4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67333;
CC Evidence={ECO:0000250|UniProtKB:Q8HYE4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deoxyglucosone + H2O + NAD(+) = 2-dehydro-3-deoxy-D-
CC gluconate + 2 H(+) + NADH; Xref=Rhea:RHEA:67244, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:57990, ChEBI:CHEBI:60777;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67245;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-hydroxynon-2-enal + H2O + NAD(+) = (E)-4-hydroxynon-2-
CC enoate + 2 H(+) + NADH; Xref=Rhea:RHEA:67248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:58968, ChEBI:CHEBI:142920;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67249;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + malonaldehyde + NAD(+) = 3-oxopropanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:67252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33190, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:566274; Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67253;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanal + NAD(+) = 2 H(+) + hexanoate + NADH;
CC Xref=Rhea:RHEA:67276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17120, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:88528; Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67277;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) + propanal = 2 H(+) + NADH + propanoate;
CC Xref=Rhea:RHEA:67256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17153, ChEBI:CHEBI:17272, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67257;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + H2O + NAD(+) = acetate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:25294, ChEBI:CHEBI:15343, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25295;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzaldehyde + H2O + NAD(+) = benzoate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:11840, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16150, ChEBI:CHEBI:17169, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.28;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11841;
CC Evidence={ECO:0000250|UniProtKB:P00352};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanal + H2O + NAD(+) = 4-aminobutanoate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:19105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58264,
CC ChEBI:CHEBI:59888; EC=1.2.1.19;
CC Evidence={ECO:0000250|UniProtKB:P24549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19106;
CC Evidence={ECO:0000250|UniProtKB:P24549};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000250|UniProtKB:P51647}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P51977}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P00352}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P24549}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X58869; CAA41679.1; -; mRNA.
DR PIR; S14629; S14629.
DR RefSeq; NP_989908.1; NM_204577.4.
DR AlphaFoldDB; P27463; -.
DR SMR; P27463; -.
DR STRING; 9031.ENSGALP00000024396; -.
DR BindingDB; P27463; -.
DR ChEMBL; CHEMBL4295737; -.
DR GeneID; 395264; -.
DR KEGG; gga:395264; -.
DR CTD; 216; -.
DR VEuPathDB; HostDB:geneid_395264; -.
DR eggNOG; KOG2450; Eukaryota.
DR InParanoid; P27463; -.
DR OrthoDB; 153834at2759; -.
DR PhylomeDB; P27463; -.
DR BRENDA; 1.2.1.36; 1306.
DR UniPathway; UPA00912; -.
DR PRO; PR:P27463; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0106373; F:3-deoxyglucosone dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0018479; F:benzaldehyde dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:RHEA.
DR GO; GO:0001758; F:retinal dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; ISS:UniProtKB.
DR GO; GO:0030392; P:fructosamine catabolic process; ISS:UniProtKB.
DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; ISS:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
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 Cell projection; Cytoplasm; Lipid metabolism; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..509
FT /note="Aldehyde dehydrogenase 1A1"
FT /id="PRO_0000056421"
FT ACT_SITE 277
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 311
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 175..178
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 201..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 234..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 254..255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 277..279
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 357..361
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT BINDING 408..410
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00352"
FT SITE 178
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P20000"
SQ SEQUENCE 509 AA; 55809 MW; 7771181FA2F05DA9 CRC64;
MKKQGSPSNP APVLPALPEP LKDLKIKYTK IFINNEWHDS VSGKKFEVFN PANEEKICEV
AEGDKADIDK AVKAARKAFE LGSPWRTMDA SERGRLLNKL ADLVERDRLT LATMEAIDGG
KLFSTAYLMD LGACIKTIRY CAGWADKIHG RTVPMDGNFF TFTRHEPVGV CGQIIPWNFP
LVMFIWKIAP ALCCGNTVVV KPAEQTPLSA LYMGSLIKEA GFPPGVVNIV PGFGPTAGAA
ISHHMDIDKV SFTGSTEVGK LIKEAAGKTN LKRVTLELGG KSPNIIFADA DLDEAAEFAH
IGLFYHQGQC CIAGSRIFVE EPIYDEFVRR SIERAKKYTL GDPLLPGVQQ GPQIDKEQFQ
KILDLIESGK KEGAKLECGG GPWGNKGYFI QPTVFSNVTD DMRIAKEEIF GPVQQIMKFK
TIDEVIKRAN NTTYGLAAAV FTKDIDKALT FASALQAGTV WVNCYSAFSA QCPFGGFKMS
GNGRELGEYG LQEYTEVKTV TIKIPQKNS
