ID   AK1A1_CHICK             Reviewed;         327 AA.
AC   Q5ZK84;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=RCJMB04_12g8;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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; AJ720200; CAG31859.1; -; mRNA.
DR   RefSeq; NP_001006539.1; NM_001006539.2.
DR   AlphaFoldDB; Q5ZK84; -.
DR   SMR; Q5ZK84; -.
DR   STRING; 9031.ENSGALP00000016630; -.
DR   PaxDb; Q5ZK84; -.
DR   GeneID; 424599; -.
DR   KEGG; gga:424599; -.
DR   CTD; 10327; -.
DR   VEuPathDB; HostDB:geneid_424599; -.
DR   eggNOG; KOG1577; Eukaryota.
DR   InParanoid; Q5ZK84; -.
DR   PhylomeDB; Q5ZK84; -.
DR   PRO; PR:Q5ZK84; -.
DR   Proteomes; UP000000539; 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   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_0000384151"
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;  37077 MW;  8B590B4F560A855B CRC64;
     MSAGCDFVAL YNGQKIPLIG LGTWKSEPGQ VKEAVKYALS VGYRHVDCAA AYSNEAEIGD
     AFQECVGPNK VIKREDLFVT SKLWNTKHHP EDVEPALRKT LADLKLDYLD LYLMHWPHAF
     ERGDNLFPKN PDGTMRYDYT DYKDTWKAME KLVEKGLAKA IGLSNFNSRQ IDDVLSVATV
     KPAVLQVECH PYLAQNELIA HCQKRGLVVT AYSPLGSPDR MWKHPDEPVL LEEPGIKKLA
     EKYKKSPAQI LLRWQAQRKV VTIPKSVTPA RILQNLQVFD FSLTEEEMSH VGSLNKNWRY
     IVPMLTVNGK PVPRDAGHPN YPFNDPY