ID   ALDX_SPOSA              Reviewed;         323 AA.
AC   P27800; Q12707;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Aldehyde reductase 1;
DE            Short=ALR 1;
DE            EC=1.1.1.2 {ECO:0000269|PubMed:1633196, ECO:0000269|PubMed:8779568};
DE   AltName: Full=Alcohol dehydrogenase [NADP(+)];
DE   AltName: Full=Aldehyde reductase I;
GN   Name=ARI;
OS   Sporidiobolus salmonicolor (Sporobolomyces salmonicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Sporidiobolus.
OX   NCBI_TaxID=5005;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-125; 133-154;
RP   157-200 AND 203-314, FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=AKU 4429;
RX   PubMed=8779568; DOI=10.1128/aem.62.7.2303-2310.1996;
RA   Kita K., Matsuzaki K., Hashimoto T., Yanase H., Kato N., Chung M.C.-M.,
RA   Kataoka M., Shimizu S.;
RT   "Cloning of the aldehyde reductase gene from a red yeast, Sporobolomyces
RT   salmonicolor, and characterization of the gene and its product.";
RL   Appl. Environ. Microbiol. 62:2303-2310(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-52, ACTIVITY REGULATION, FUNCTION, CATALYTIC
RP   ACTIVITY, AND SUBUNIT.
RC   STRAIN=AKU 4429;
RX   PubMed=1633196; DOI=10.1016/0167-4838(92)90127-y;
RA   Kataoka M., Sakai H., Morikawa T., Katoh M., Miyoshi T., Shimizu S.,
RA   Yamada H.;
RT   "Characterization of aldehyde reductase of Sporobolomyces salmonicolor.";
RL   Biochim. Biophys. Acta 1122:57-62(1992).
CC   -!- FUNCTION: Catalyzes the asymmetric reduction of aliphatic and aromatic
CC       aldehydes and ketones to an R-enantiomer. Reduces ethyl 4-chloro-3-
CC       oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate.
CC       {ECO:0000269|PubMed:1633196, ECO:0000269|PubMed:8779568}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
CC         Evidence={ECO:0000269|PubMed:1633196, ECO:0000269|PubMed:8779568};
CC   -!- ACTIVITY REGULATION: Inhibited by quercetin, dicoumarol and some SH-
CC       reagents. {ECO:0000269|PubMed:1633196}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1633196}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR   EMBL; U26463; AAB17362.1; -; Genomic_DNA.
DR   PIR; S78113; S78113.
DR   AlphaFoldDB; P27800; -.
DR   SMR; P27800; -.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR   CDD; cd19118; AKR_AKR3B1-3; 1.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR020471; AKR.
DR   InterPro; IPR044490; AKR3B.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PIRSF; PIRSF000097; AKR; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   SUPFAM; SSF51430; SSF51430; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1633196"
FT   CHAIN           2..323
FT                   /note="Aldehyde reductase 1"
FT                   /id="PRO_0000124621"
FT   ACT_SITE        49
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         210..267
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            74
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   323 AA;  35339 MW;  D49B33ACB41D4D60 CRC64;
     MVGTTTLNTG ASLELVGYGT WQAAPGEVGQ GVKVAIETGY RHLDLAKVYS NQPEVGAAIK
     EAGVKREDLF ITSKLWNNSH RPEQVEPALD DTLKELGLEY LDLYLIHWPV AFPPEGDITQ
     NLFPKANDKE VKLDLEVSLV DTWKAMVKLL DTGKVKAIGV SNFDAKMVDA IIEATGVTPS
     VNQIERHPLL LQPELIAHHK AKNIHITAYS PLGNNTVGAP LLVQHPEIKR IAEKNGCTPA
     QVLIAWAIVG GHSVIPKSVT PSRIGENFKQ VSLSQEDVDA VSKLGEGSGR RRYNIPCTYS
     PKWDINVFGE EDEKSCKNAV KIK