ID   AK1A1_XENTR             Reviewed;         327 AA.
AC   Q28FD1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Aldo-keto reductase family 1 member A1;
DE            EC=1.1.1.2 {ECO:0000250|UniProtKB:P14550};
DE   AltName: Full=Alcohol dehydrogenase [NADP(+)];
DE   AltName: Full=Aldehyde reductase;
GN   Name=akr1a1; ORFNames=TEgg056i02.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neurula;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2008) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR762028; CAJ81495.1; -; mRNA.
DR   EMBL; BC170750; AAI70750.1; -; mRNA.
DR   EMBL; BC170752; AAI70752.1; -; mRNA.
DR   RefSeq; NP_001016137.1; NM_001016137.2.
DR   RefSeq; XP_012816517.1; XM_012961063.2.
DR   RefSeq; XP_012816518.1; XM_012961064.2.
DR   RefSeq; XP_012816520.1; XM_012961066.2.
DR   RefSeq; XP_012816521.1; XM_012961067.2.
DR   RefSeq; XP_017948526.1; XM_018093037.1.
DR   AlphaFoldDB; Q28FD1; -.
DR   SMR; Q28FD1; -.
DR   PaxDb; Q28FD1; -.
DR   Ensembl; ENSXETT00000007570; ENSXETP00000007570; ENSXETG00000003499.
DR   GeneID; 548891; -.
DR   KEGG; xtr:548891; -.
DR   CTD; 10327; -.
DR   Xenbase; XB-GENE-1014353; akr1a1.
DR   eggNOG; KOG1577; Eukaryota.
DR   HOGENOM; CLU_023205_0_0_1; -.
DR   InParanoid; Q28FD1; -.
DR   OMA; AMFTEIK; -.
DR   OrthoDB; 1016440at2759; -.
DR   PhylomeDB; Q28FD1; -.
DR   TreeFam; TF106492; -.
DR   Reactome; R-XTR-156590; Glutathione conjugation.
DR   Reactome; R-XTR-5661270; Formation of xylulose-5-phosphate.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000003499; Expressed in mesonephros and 16 other tissues.
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   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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; Lipid metabolism; Membrane; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..327
FT                   /note="Aldo-keto reductase family 1 member A1"
FT                   /id="PRO_0000384155"
FT   ACT_SITE        52
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P14550"
FT   BINDING         115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P14550"
FT   BINDING         213..275
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            82
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250|UniProtKB:P14550"
SQ   SEQUENCE   327 AA;  37064 MW;  8B5CB49726E4FBCC CRC64;
     MATAVEYETL YTGQKIPLIG LGTWKSAPGQ VKDAVKYALG VGYRHIDCAF VYGNETEVGE
     AIKESVGSDK GLSREEVFVT SKLWNNKHHP DDVECALRKT LQDLQLDYLD LYLMHWPYAF
     KRGDQIFPQN PDGSVQYDLT DYKDTWKAME KLVKQGLTKA IGLSNFNKRQ IDDIISIATV
     KPAVLQVECH PYLAQNELIA YCHAHGLVFT GYSPLGSPDR SWRKPEDPVL LEEPGIIAMA
     KKYGKSEAQI LLRWQVQRKV VSIPKSVTPT RILQNFQVFD FSLSEEEMQL IGALNKNWRY
     IIPLITVNGK SVPRDAGHPL YPFNDPY