ALD2_SPOSA
ID ALD2_SPOSA Reviewed; 343 AA.
AC Q9UUN9;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Aldehyde reductase 2;
DE EC=1.1.1.2;
DE AltName: Full=Aldehyde reductase II;
DE Short=ARII;
OS Sporidiobolus salmonicolor (Sporobolomyces salmonicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Sporidiobolus.
OX NCBI_TaxID=5005 {ECO:0000312|EMBL:AAF15999.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 39-54; 75-83;
RP 153-161; 182-184 AND 336-343, MUTAGENESIS OF GLY-19; GLY-22 AND ALA-25, AND
RP FUNCTION.
RC STRAIN=AKU 4429;
RX PubMed=10583966; DOI=10.1128/aem.65.12.5207-5211.1999;
RA Kita K., Fukura T., Nakase K., Okamoto K., Yanase H., Kataoka M.,
RA Shimizu S.;
RT "Cloning, overexpression, and mutagenesis of the Sporobolomyces
RT salmonicolor AKU4429 gene encoding a new aldehyde reductase, which
RT catalyzes the stereoselective reduction of ethyl 4-chloro-3-oxobutanoate to
RT ethyl (S)-4-chloro-3-hydroxybutanoate.";
RL Appl. Environ. Microbiol. 65:5207-5211(1999).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-25, FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=AKU 4429;
RA Kita K., Nakase K., Yanase H., Kataoka M., Shimizu S.;
RT "Purification and characterization of new aldehyde reductases from
RT Sporobolomyces salmonicolor AKU4429.";
RL J. Mol. Catal., B Enzym. 6:305-313(1999).
CC -!- FUNCTION: Catalyzes the asymmetric reduction of o-substituted aliphatic
CC and aromatic aldehydes and ketones to an S-enantiomer. Reduces ethyl 4-
CC chloro-3-oxobutanoate to ethyl (S)-4-chloro-3-hydroxybutanoate.
CC {ECO:0000269|PubMed:10583966, ECO:0000269|Ref.2}.
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:10583966, ECO:0000269|Ref.2};
CC -!- ACTIVITY REGULATION: Inhibited by quercetin and diphenylhydantoin.
CC {ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5.;
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily. {ECO:0000305}.
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DR EMBL; AF160799; AAF15999.1; -; Genomic_DNA.
DR PDB; 1UJM; X-ray; 2.00 A; A/B=2-343.
DR PDB; 1Y1P; X-ray; 1.60 A; A/B=2-343.
DR PDB; 1ZZE; X-ray; 1.80 A; A/B=2-343.
DR PDBsum; 1UJM; -.
DR PDBsum; 1Y1P; -.
DR PDBsum; 1ZZE; -.
DR AlphaFoldDB; Q9UUN9; -.
DR SMR; Q9UUN9; -.
DR EvolutionaryTrace; Q9UUN9; -.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; NADP; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..343
FT /note="Aldehyde reductase 2"
FT /id="PRO_0000215575"
FT BINDING 177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:A0A059TC02"
FT MUTAGEN 19
FT /note="G->A: Results in loss of substrate inhibition and of
FT NADPH-dependent reductase activity."
FT /evidence="ECO:0000269|PubMed:10583966"
FT MUTAGEN 22
FT /note="G->A: Results in loss of substrate inhibition and of
FT NADPH-dependent reductase activity."
FT /evidence="ECO:0000269|PubMed:10583966"
FT MUTAGEN 25
FT /note="A->G: Only active when NADPH is replaced by NADH."
FT /evidence="ECO:0000269|PubMed:10583966"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:1Y1P"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:1Y1P"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:1Y1P"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1Y1P"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:1Y1P"
FT TURN 75..84
FT /evidence="ECO:0007829|PDB:1Y1P"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 101..120
FT /evidence="ECO:0007829|PDB:1Y1P"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 172..195
FT /evidence="ECO:0007829|PDB:1Y1P"
FT STRAND 198..210
FT /evidence="ECO:0007829|PDB:1Y1P"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:1Y1P"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:1Y1P"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1Y1P"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 313..321
FT /evidence="ECO:0007829|PDB:1Y1P"
FT HELIX 330..338
FT /evidence="ECO:0007829|PDB:1Y1P"
SQ SEQUENCE 343 AA; 37318 MW; C6CAAD9DB32E05C3 CRC64;
MAKIDNAVLP EGSLVLVTGA NGFVASHVVE QLLEHGYKVR GTARSASKLA NLQKRWDAKY
PGRFETAVVE DMLKQGAYDE VIKGAAGVAH IASVVSFSNK YDEVVTPAIG GTLNALRAAA
ATPSVKRFVL TSSTVSALIP KPNVEGIYLD EKSWNLESID KAKTLPESDP QKSLWVYAAS
KTEAELAAWK FMDENKPHFT LNAVLPNYTI GTIFDPETQS GSTSGWMMSL FNGEVSPALA
LMPPQYYVSA VDIGLLHLGC LVLPQIERRR VYGTAGTFDW NTVLATFRKL YPSKTFPADF
PDQGQDLSKF DTAPSLEILK SLGRPGWRSI EESIKDLVGS ETA
