A1A1B_DANRE
ID A1A1B_DANRE Reviewed; 324 AA.
AC Q568L5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Aldo-keto reductase family 1 member A1-B;
DE EC=1.1.1.2 {ECO:0000250|UniProtKB:P14550};
DE AltName: Full=Alcohol dehydrogenase [NADP(+)] B;
DE AltName: Full=Aldehyde reductase-B;
GN Name=akr1a1b; ORFNames=zgc:110225;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of
CC carbonyl-containing compounds to their corresponding alcohols. Displays
CC enzymatic activity towards endogenous metabolites such as aromatic and
CC aliphatic aldehydes, ketones, monosaccharides and bile acids. Acts as
CC an aldehyde-detoxification enzyme (By similarity). Displays no
CC reductase activity towards retinoids (By similarity).
CC {ECO:0000250|UniProtKB:P14550, ECO:0000250|UniProtKB:P50578,
CC ECO:0000250|UniProtKB:P51635}.
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:0000250|UniProtKB:P14550};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JII6}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9JII6}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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DR EMBL; BC092808; AAH92808.1; -; mRNA.
DR EMBL; BC155150; AAI55151.1; -; mRNA.
DR RefSeq; NP_001017640.1; NM_001017640.1.
DR AlphaFoldDB; Q568L5; -.
DR SMR; Q568L5; -.
DR STRING; 7955.ENSDARP00000119785; -.
DR PaxDb; Q568L5; -.
DR PeptideAtlas; Q568L5; -.
DR GeneID; 799805; -.
DR KEGG; dre:799805; -.
DR CTD; 799805; -.
DR ZFIN; ZDB-GENE-050417-118; akr1a1b.
DR eggNOG; KOG1577; Eukaryota.
DR InParanoid; Q568L5; -.
DR OrthoDB; 1016440at2759; -.
DR PhylomeDB; Q568L5; -.
DR Reactome; R-DRE-156590; Glutathione conjugation.
DR Reactome; R-DRE-5661270; Formation of xylulose-5-phosphate.
DR PRO; PR:Q568L5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0046185; P:aldehyde catabolic process; IEA:InterPro.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; ISS:UniProtKB.
DR CDD; cd19106; AKR_AKR1A1-4; 1.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR044481; AKR1A.
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.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Membrane; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..324
FT /note="Aldo-keto reductase family 1 member A1-B"
FT /id="PRO_0000384153"
FT ACT_SITE 49
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P14550"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P14550"
FT BINDING 210..272
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 79
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:P14550"
SQ SEQUENCE 324 AA; 36818 MW; 03DCF80D56D59F6C CRC64;
MNDFAVLSTG RKMPLLGLGT WKSEPGLVKQ AVIWALESGY RHIDCAPIYA NEPEIGEAFQ
ETMGPDKGIR REDVFVTSKL WNTKHHPDDV EPSLLKTLKD LKLEYLDLYL IHWPYAFQRG
DTPFPRKEDG TLLYDDIDYK LTWAAMEKLV GKGLVRAIGL SNFNSRQIDD ILSVASIKPT
VLQVESHPYL AQVELLSHCR DRGLVMTAYS PLGSPDRAWK HPDEPVLLEE PAIAALAKKY
NKTPAQIIIR WQTQRGVVTI PKSITQSRIK ENIQVFDFTL ESEEMSQVTA LHRGWRYIVP
TITVDGKSVP RDAGHPHYPF NDPY
