ID G8F2B0_MACFA Unreviewed; 325 AA.
AC G8F2B0;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Aldo-keto reductase family 1 member A1 {ECO:0000256|ARBA:ARBA00024099};
DE EC=1.1.1.19 {ECO:0000256|ARBA:ARBA00024067};
DE EC=1.1.1.2 {ECO:0000256|ARBA:ARBA00024074};
DE EC=1.1.1.20 {ECO:0000256|ARBA:ARBA00024068};
DE EC=1.1.1.372 {ECO:0000256|ARBA:ARBA00024066};
DE EC=1.1.1.54 {ECO:0000256|ARBA:ARBA00024070};
DE AltName: Full=Alcohol dehydrogenase [NADP(+)] {ECO:0000256|ARBA:ARBA00032111};
DE AltName: Full=Aldehyde reductase {ECO:0000256|ARBA:ARBA00029846};
DE AltName: Full=Glucuronate reductase {ECO:0000256|ARBA:ARBA00033112};
DE AltName: Full=Glucuronolactone reductase {ECO:0000256|ARBA:ARBA00032421};
GN Name=AKR1A1 {ECO:0000313|Ensembl:ENSMFAP00000031452.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000031452.1, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000031452.1, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000031452.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-deoxyfructose + NADP(+) = 3-deoxyglucosone + H(+) + NADPH;
CC Xref=Rhea:RHEA:58668, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:60777, ChEBI:CHEBI:142685;
CC Evidence={ECO:0000256|ARBA:ARBA00023987};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-gulonate + NADP(+) = aldehydo-D-glucuronate + H(+) + NADPH;
CC Xref=Rhea:RHEA:14909, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:142686;
CC EC=1.1.1.19; Evidence={ECO:0000256|ARBA:ARBA00023919};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone +
CC H(+) + NADPH; Xref=Rhea:RHEA:18925, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17587, ChEBI:CHEBI:18268, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.1.1.20;
CC Evidence={ECO:0000256|ARBA:ARBA00023969};
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:0000256|ARBA:ARBA00023978};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=allyl alcohol + NADP(+) = acrolein + H(+) + NADPH;
CC Xref=Rhea:RHEA:12168, ChEBI:CHEBI:15368, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16605, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.54;
CC Evidence={ECO:0000256|ARBA:ARBA00023997};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NADP(+) = D-glyceraldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:23592, ChEBI:CHEBI:15378, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.372; Evidence={ECO:0000256|ARBA:ARBA00023947};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycerol + NADP(+) = H(+) + L-glyceraldehyde + NADPH;
CC Xref=Rhea:RHEA:38111, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:27975, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.372; Evidence={ECO:0000256|ARBA:ARBA00023958};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydroxyacetone + NADP(+) = H(+) + methylglyoxal + NADPH;
CC Xref=Rhea:RHEA:27986, ChEBI:CHEBI:15378, ChEBI:CHEBI:17158,
CC ChEBI:CHEBI:27957, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC Evidence={ECO:0000256|ARBA:ARBA00024000};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000256|ARBA:ARBA00004221}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family.
CC {ECO:0000256|ARBA:ARBA00007905}.
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 RefSeq; XP_005595646.1; XM_005595589.2.
DR RefSeq; XP_005595647.1; XM_005595590.2.
DR RefSeq; XP_005595648.1; XM_005595591.1.
DR RefSeq; XP_005595649.1; XM_005595592.2.
DR AlphaFoldDB; G8F2B0; -.
DR SMR; G8F2B0; -.
DR Ensembl; ENSMFAT00000005668.2; ENSMFAP00000031452.1; ENSMFAG00000036808.2.
DR GeneID; 102143796; -.
DR KEGG; mcf:102143796; -.
DR CTD; 10327; -.
DR VEuPathDB; HostDB:ENSMFAG00000036808; -.
DR eggNOG; KOG1577; Eukaryota.
DR GeneTree; ENSGT00940000156539; -.
DR OMA; MVNQIFL; -.
DR OrthoDB; 890110at2759; -.
DR Proteomes; UP000233100; Chromosome 1.
DR Bgee; ENSMFAG00000036808; Expressed in adult mammalian kidney and 13 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0004032; F:alditol:NADP+ 1-oxidoreductase activity; IEA:Ensembl.
DR GO; GO:0047655; F:allyl-alcohol dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0047941; F:glucuronolactone reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0047939; F:L-glucuronate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016657; F:oxidoreductase activity, acting on NAD(P)H, nitrogenous group as acceptor; IEA:Ensembl.
DR GO; GO:0046185; P:aldehyde catabolic process; IEA:Ensembl.
DR GO; GO:0110095; P:cellular detoxification of aldehyde; IEA:Ensembl.
DR GO; GO:0042840; P:D-glucuronate catabolic process; IEA:Ensembl.
DR GO; GO:0044597; P:daunorubicin metabolic process; IEA:Ensembl.
DR GO; GO:0044598; P:doxorubicin metabolic process; IEA:Ensembl.
DR GO; GO:0019640; P:glucuronate catabolic process to xylulose 5-phosphate; IEA:Ensembl.
DR GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd19106; AKR_AKR1A1-4; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 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 PANTHER; PTHR11732:SF544; ALDO-KETO REDUCTASE FAMILY 1 MEMBER A1; 1.
DR PANTHER; PTHR11732; ALDO/KETO REDUCTASE; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PIRSF; PIRSF000097; AKR; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00798; ALDOKETO_REDUCTASE_1; 1.
DR PROSITE; PS00062; ALDOKETO_REDUCTASE_2; 1.
DR PROSITE; PS00063; ALDOKETO_REDUCTASE_3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100}.
FT DOMAIN 17..293
FT /note="NADP-dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00248"
FT ACT_SITE 50
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-1"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-2"
FT SITE 80
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR000097-3"
SQ SEQUENCE 325 AA; 36631 MW; 4ABE446FB458FA34 CRC64;
MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAVKYALSVG YRHIDCAAIY GNEPEIGEAL
KEDVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER
GDNPFPKNAD GTICYDSTHY KETWKALEAL VAKGLVRALG LSNFNSRQID DILSVASVRP
AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RDPDEPVLLE EPVVLALAEK
YGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIKVFDFT FSPEEMKQLN ALNKNWRYIV
PMLMVDGKRV PRDAGHPLYP FNDPY
//
