ALDH1_ELEED
ID ALDH1_ELEED Reviewed; 501 AA.
AC Q28399;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 Elephantulus edwardii (Cape long-eared elephant shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Macroscelidea; Macroscelididae; Elephantulus.
OX NCBI_TaxID=28737;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, AND
RP HOMOTETRAMERIZATION.
RX PubMed=12693930; DOI=10.1021/bi027367w;
RA Bateman O.A., Purkiss A.G., van Montfort R., Slingsby C., Graham C.,
RA Wistow G.;
RT "Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde
RT dehydrogenase for a new role in the eye lens.";
RL Biochemistry 42:4349-4356(2003).
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 {ECO:0000269|PubMed:12693930}.
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:0000269|PubMed:12693930}.
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; U02483; AAB60268.1; -; mRNA.
DR RefSeq; NP_001277088.1; NM_001290159.1.
DR PDB; 1O9J; X-ray; 2.40 A; A/B/C/D=1-501.
DR PDBsum; 1O9J; -.
DR AlphaFoldDB; Q28399; -.
DR SMR; Q28399; -.
DR MoonProt; Q28399; -.
DR GeneID; 102867337; -.
DR CTD; 102867337; -.
DR OrthoDB; 500317at2759; -.
DR BRENDA; 1.2.1.36; 7360.
DR UniPathway; UPA00780; UER00768.
DR EvolutionaryTrace; Q28399; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
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:0042802; F:identical protein binding; IPI:CAFA.
DR GO; GO:0051287; F:NAD binding; IDA:CAFA.
DR GO; GO:0001758; F:retinal dehydrogenase activity; IDA:CAFA.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042574; P:retinal metabolic process; IDA:CAFA.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; NAD; Oxidoreductase.
FT CHAIN 1..501
FT /note="Aldehyde dehydrogenase, cytosolic 1"
FT /id="PRO_0000056427"
FT ACT_SITE 269
FT /note="Proton acceptor"
FT ACT_SITE 303
FT /note="Nucleophile"
FT BINDING 246..251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:12693930"
FT SITE 170
FT /note="Transition state stabilizer"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:1O9J"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 57..71
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 122..136
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1O9J"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 284..296
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 297..300
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 348..364
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 395..398
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 428..433
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 437..446
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 479..483
FT /evidence="ECO:0007829|PDB:1O9J"
FT HELIX 484..486
FT /evidence="ECO:0007829|PDB:1O9J"
FT STRAND 487..495
FT /evidence="ECO:0007829|PDB:1O9J"
SQ SEQUENCE 501 AA; 54538 MW; 9E3D5BBE083ACAD7 CRC64;
MSSSGMPDLP APLTNIKIQH TKLFINNEWH ESVSGKTFPV FNPATEEKIC EVEEADKEDV
DKAVKAAREA FQMGSPWRTM DASERGQLIY KLADLIERDR LLLATLESIN AGKVFASAYL
MDLDYCIKAL RYCAGWADKI QGRTIPVDGE FFSYTRHEPI GVCGLIFPWN APMILLACKI
GPALCCGNTV IVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD
KVAFTGSTEV GKMIQEAAAK SNLKRVTLEL GAKNPCIVFA DADLDSAVEF AHQGVFTNQG
QSCIAASKLF VEEAIYDEFV QRSVERAKKY VFGNPLTPGV NHGPQINKAQ HNKIMELIES
GKKEGAKLEC GGGPWGNKGY FIQPTVFSNV TDDMRIAKEE IFGPVQQIMK FKSLDEVIKR
ANNTYYGLVA GVFTKDLDKA VTVSSALQAG TVWVNCYLAA SAQSPAGGFK MSGHGREMGE
YGIHEYTEVK TVTMKISEKN S
