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Aldehyde dehydrogenase, cytosolic 1 (EC 1.2.1.3) (ALDH class 1) (ETA-crystallin)

 ALDH1_ELEED             Reviewed;         501 AA.
Q28399;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-MAY-2017, entry version 94.
RecName: Full=Aldehyde dehydrogenase, cytosolic 1;
EC=1.2.1.3;
AltName: Full=ALDH class 1;
AltName: Full=ETA-crystallin;
Name=ALDH1;
Elephantulus edwardii (Cape long-eared elephant shrew).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Afrotheria; Macroscelidea; Macroscelididae;
Elephantulus.
NCBI_TaxID=28737;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lens;
PubMed=8663049; DOI=10.1074/jbc.271.26.15623;
Graham C., Hodin J., Wistow G.;
"A retinaldehyde dehydrogenase as a structural protein in a mammalian
eye lens. Gene recruitment of eta-crystallin.";
J. Biol. Chem. 271:15623-15628(1996).
[2]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION,
AND HOMOTETRAMERIZATION.
PubMed=12693930; DOI=10.1021/bi027367w;
Bateman O.A., Purkiss A.G., van Montfort R., Slingsby C., Graham C.,
Wistow G.;
"Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde
dehydrogenase for a new role in the eye lens.";
Biochemistry 42:4349-4356(2003).
-!- FUNCTION: Major component of the eye of elephant shrews, which in
contrast to other mammals, possesses both a lens- and a non-lens
class-1 aldehyde dehydrogenase 1. This eye-specific form is a
structural protein of the lens and, in other part of the eye,
serves as the major form of ALDH1. Can convert/oxidize
retinaldehyde to retinoic acid. {ECO:0000269|PubMed:12693930}.
-!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = a carboxylate +
NADH.
-!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from
ethanol: step 2/2.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:12693930}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Eye specific, with very high expression in the
lens.
-!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
{ECO:0000305}.
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EMBL; U02483; AAB60268.1; -; mRNA.
RefSeq; NP_001277088.1; NM_001290159.1.
PDB; 1O9J; X-ray; 2.40 A; A/B/C/D=1-501.
PDB; 1PEJ; Model; -; A=1-501.
PDBsum; 1O9J; -.
PDBsum; 1PEJ; -.
ProteinModelPortal; Q28399; -.
SMR; Q28399; -.
PRIDE; Q28399; -.
GeneID; 102867337; -.
CTD; 102867337; -.
HOVERGEN; HBG000097; -.
OrthoDB; EOG091G05E8; -.
BRENDA; 1.2.1.36; 7360.
UniPathway; UPA00780; UER00768.
EvolutionaryTrace; Q28399; -.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:UniProtKB-EC.
GO; GO:0051287; F:NAD binding; IDA:CAFA.
GO; GO:0001758; F:retinal dehydrogenase activity; IDA:CAFA.
GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
GO; GO:0051289; P:protein homotetramerization; IDA:CAFA.
GO; GO:0042574; P:retinal metabolic process; IDA:CAFA.
Gene3D; 3.40.605.10; -; 1.
InterPro; IPR016161; Ald_DH/histidinol_DH.
InterPro; IPR016160; Ald_DH_CS_CYS.
InterPro; IPR016162; Ald_DH_N.
InterPro; IPR015590; Aldehyde_DH_dom.
Pfam; PF00171; Aldedh; 1.
SUPFAM; SSF53720; SSF53720; 1.
PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
1: Evidence at protein level;
3D-structure; Cytoplasm; NAD; Oxidoreductase.
CHAIN 1 501 Aldehyde dehydrogenase, cytosolic 1.
/FTId=PRO_0000056427.
NP_BIND 246 251 NAD. {ECO:0000269|PubMed:12693930}.
ACT_SITE 269 269 Proton acceptor.
ACT_SITE 303 303 Nucleophile.
SITE 170 170 Transition state stabilizer.
STRAND 22 25 {ECO:0000244|PDB:1O9J}.
STRAND 28 30 {ECO:0000244|PDB:1O9J}.
STRAND 37 41 {ECO:0000244|PDB:1O9J}.
TURN 43 45 {ECO:0000244|PDB:1O9J}.
STRAND 48 53 {ECO:0000244|PDB:1O9J}.
HELIX 57 71 {ECO:0000244|PDB:1O9J}.
HELIX 76 79 {ECO:0000244|PDB:1O9J}.
HELIX 82 98 {ECO:0000244|PDB:1O9J}.
HELIX 100 111 {ECO:0000244|PDB:1O9J}.
HELIX 115 120 {ECO:0000244|PDB:1O9J}.
HELIX 122 136 {ECO:0000244|PDB:1O9J}.
HELIX 137 139 {ECO:0000244|PDB:1O9J}.
STRAND 142 145 {ECO:0000244|PDB:1O9J}.
STRAND 148 159 {ECO:0000244|PDB:1O9J}.
STRAND 162 166 {ECO:0000244|PDB:1O9J}.
HELIX 172 185 {ECO:0000244|PDB:1O9J}.
STRAND 189 193 {ECO:0000244|PDB:1O9J}.
HELIX 200 212 {ECO:0000244|PDB:1O9J}.
STRAND 218 221 {ECO:0000244|PDB:1O9J}.
TURN 226 228 {ECO:0000244|PDB:1O9J}.
HELIX 229 234 {ECO:0000244|PDB:1O9J}.
STRAND 241 246 {ECO:0000244|PDB:1O9J}.
HELIX 248 260 {ECO:0000244|PDB:1O9J}.
STRAND 265 269 {ECO:0000244|PDB:1O9J}.
STRAND 274 278 {ECO:0000244|PDB:1O9J}.
HELIX 284 296 {ECO:0000244|PDB:1O9J}.
HELIX 297 300 {ECO:0000244|PDB:1O9J}.
STRAND 306 312 {ECO:0000244|PDB:1O9J}.
HELIX 313 326 {ECO:0000244|PDB:1O9J}.
HELIX 348 364 {ECO:0000244|PDB:1O9J}.
STRAND 367 370 {ECO:0000244|PDB:1O9J}.
STRAND 373 379 {ECO:0000244|PDB:1O9J}.
STRAND 385 390 {ECO:0000244|PDB:1O9J}.
HELIX 395 398 {ECO:0000244|PDB:1O9J}.
STRAND 403 411 {ECO:0000244|PDB:1O9J}.
HELIX 414 422 {ECO:0000244|PDB:1O9J}.
STRAND 423 425 {ECO:0000244|PDB:1O9J}.
STRAND 428 433 {ECO:0000244|PDB:1O9J}.
HELIX 437 446 {ECO:0000244|PDB:1O9J}.
STRAND 449 455 {ECO:0000244|PDB:1O9J}.
HELIX 470 472 {ECO:0000244|PDB:1O9J}.
STRAND 473 475 {ECO:0000244|PDB:1O9J}.
HELIX 479 483 {ECO:0000244|PDB:1O9J}.
HELIX 484 486 {ECO:0000244|PDB:1O9J}.
STRAND 487 495 {ECO:0000244|PDB:1O9J}.
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


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