ID   ALDH1_MACPR             Reviewed;         501 AA.
AC   Q29490;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Aldehyde dehydrogenase, cytosolic 1;
DE            EC=1.2.1.3;
DE   AltName: Full=ALDH class 1;
DE   AltName: Full=ETA-crystallin;
GN   Name=ALDH1;
OS   Macroscelides proboscideus (Short-eared elephant shrew).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Macroscelidea; Macroscelididae; Macroscelides.
OX   NCBI_TaxID=29082;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Eye;
RX   PubMed=8663049; DOI=10.1074/jbc.271.26.15623;
RA   Graham C., Hodin J., Wistow G.;
RT   "A retinaldehyde dehydrogenase as a structural protein in a mammalian eye
RT   lens. Gene recruitment of eta-crystallin.";
RL   J. Biol. Chem. 271:15623-15628(1996).
CC   -!- FUNCTION: Major component of the eye of elephant shrews, which in
CC       contrast to other mammals, possesses both a lens- and a non-lens class-
CC       1 aldehyde dehydrogenase 1. This eye-specific form is a structural
CC       protein of the lens and, in other part of the eye, serves as the major
CC       form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid.
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   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC       step 2/2.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Eye specific, with very high expression in the
CC       lens.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; U03906; AAC48588.1; -; mRNA.
DR   AlphaFoldDB; Q29490; -.
DR   SMR; Q29490; -.
DR   UniPathway; UPA00780; UER00768.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; ISS:CAFA.
DR   GO; GO:0006068; P:ethanol catabolic 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; 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.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN           1..501
FT                   /note="Aldehyde dehydrogenase, cytosolic 1"
FT                   /id="PRO_0000056428"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         246..251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            170
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  54625 MW;  48C15C682665D0C0 CRC64;
     MSSSGMPDLP APLTNIKIQH TKLFINNEWH DSVSGKTFPV FNPATEEKIC EVEEADKEDV
     DKAVKAAREA FQMGSPWRTM DASERGQLIY KLADLIERDR LLLATLESIN AGKIFASAYL
     MDLDYCIKVL RYCAGWADKI QGRTIPVDGE FFSYTRHEPI GVCGQIFPWN APMILLACKI
     GPALCCGNTV IVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD
     KVAFTGSTEV GKMIQEAAAK SNLKRVTLEL GAKNPCIVFA DADLDSAVEF AHQGVFTNQG
     QSCIAASKLF VEETIYDEFV QRSVERAKKY VFGNPLTPGV NHGPQINKAQ HNKIMELIES
     GKKEGAKLEC GGGPWGNKGY FIQPTIFSNV TDDMRIAKEE IFGPVQQIMK FKSLDEVIKR
     ANNTYYGLVA GVFTKDLDKA VTVSSALQAG TVWVNCYLAA SAQSPAGGFK MSGHGREMGE
     YGIHEYTEVK TVTMKISEKN S