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   25-NOV-2008, entry version 59.
DE   RecName: Full=Aldehyde reductase 1;
DE            Short=ALR 1;
DE            EC=1.1.1.2;
DE   AltName: Full=Aldehyde reductase I;
DE   AltName: Full=Alcohol dehydrogenase [NADP+];
GN   Name=ARI;
OS   Sporobolomyces salmonicolor.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolus.
OX   NCBI_TaxID=5005;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-125;
RP   133-154; 157-200 AND 203-314, AND FUNCTION.
RC   STRAIN=AKU 4429;
RX   MEDLINE=96271678; PubMed=8779568;
RA   Kita K., Matsuzaki K., Hashimoto T., Yanase H., Kato N.,
RA   Chung M.C.-M., Kataoka M., Shimizu S.;
RT   "Cloning of the aldehyde reductase gene from a red yeast,
RT   Sporobolomyces salmonicolor, and characterization of the gene and its
RT   product.";
RL   Appl. Environ. Microbiol. 62:2303-2310(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-52, AND ENZYME REGULATION.
RC   STRAIN=AKU 4429;
RX   MEDLINE=92338224; 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
RT   salmonicolor.";
RL   Biochim. Biophys. Acta 1122:57-62(1992).
CC   -!- FUNCTION: Catalyzes the asymmetric reduction of aliphatic and
CC       aromatic aldehydes and ketones to an R-enantiomer. Reduces ethyl
CC       4-chloro-3-oxobutanoate to ethyl (R)-4-chloro-3-hydroxybutanoate.
CC   -!- CATALYTIC ACTIVITY: An alcohol + NADP(+) = an aldehyde + NADPH.
CC   -!- ENZYME REGULATION: Inhibited by quercetin, dicoumarol and some SH-
CC       reagents.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
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DR   EMBL; U26463; AAB17362.1; -; Genomic_DNA.
DR   PIR; S78113; S78113.
DR   HSSP; P14550; 2ALR.
DR   GO; GO:0005623; C:cell; IDA:UniProtKB.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001395; Aldo/ket_red.
DR   Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732; Aldo/ket_red; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PRINTS; PR00069; ALDKETRDTASE.
DR   ProDom; PD000288; Aldo/ket_red; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    323       Aldehyde reductase 1.
FT                                /FTId=PRO_0000124621.
FT   NP_BIND     210    267       NADP (By similarity).
FT   ACT_SITE     49     49       Proton donor (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   SITE         74     74       Lowers pKa of active site Tyr (By
FT                                similarity).
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
//