UniProtKB - P50578 (AK1A1_PIG)
Aldo-keto reductase family 1 member A1
AKR1A1
Functioni
Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a preference for negatively charged substrates, such as glucuronate and succinic semialdehyde (By similarity).
Plays an important role in ascorbic acid biosynthesis by catalyzing the reduction of D-glucuronic acid and D-glucurono-gamma-lactone (By similarity).
Functions as a detoxifiying enzyme by reducing a range of toxic aldehydes. Reduces methylglyoxal and 3-deoxyglucosone, which are present at elevated levels under hyperglycemic conditions and are cytotoxic. Involved also in the detoxification of lipid-derived aldehydes like acrolein (By similarity).
Plays a role in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs (By similarity).
Displays no reductase activity towards retinoids (PubMed:12732097).
By similarity1 PublicationCatalytic activityi
- EC:1.1.1.21 Publication
- EC:1.1.1.3721 Publication
- EC:1.1.1.3721 Publication
- EC:1.1.1.19By similarity
- EC:1.1.1.20By similarity
- EC:1.1.1.54By similarity
- EC:1.1.1.33By similarity
Kineticsi
- KM=700 µM for pyridine-3-carbaldehyde1 Publication
- KM=4600 µM for D,L-glyceraldehyde1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 45 | NADPBy similarity | 1 | |
Active sitei | 50 | Proton donor1 Publication | 1 | |
Sitei | 80 | Lowers pKa of active site TyrBy similarity | 1 | |
Binding sitei | 113 | Substrate1 Publication | 1 | |
Binding sitei | 184 | NADPBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 11 – 20 | NADPSequence analysis | 10 | |
Nucleotide bindingi | 21 – 23 | NADPBy similarity | 3 | |
Nucleotide bindingi | 162 – 163 | NADPBy similarity | 2 | |
Nucleotide bindingi | 211 – 273 | NADP1 PublicationAdd BLAST | 63 |
GO - Molecular functioni
- alditol:NADP+ 1-oxidoreductase activity Source: GO_Central
- allyl-alcohol dehydrogenase activity Source: UniProtKB-EC
- glucuronolactone reductase activity Source: UniProtKB
- glycerol dehydrogenase [NADP+] activity Source: RHEA
- L-glucuronate reductase activity Source: UniProtKB
- methylglyoxal reductase (NADPH-dependent, acetol producing) Source: RHEA
- mevaldate reductase (NADPH) activity Source: UniProtKB-EC
GO - Biological processi
- aldehyde catabolic process Source: InterPro
- cellular detoxification of aldehyde Source: UniProtKB
- D-glucuronate catabolic process Source: UniProtKB
- L-ascorbic acid biosynthetic process Source: UniProtKB
- lipid metabolic process Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase |
Biological process | Lipid metabolism |
Ligand | NADP |
Enzyme and pathway databases
BRENDAi | 1.1.1.2, 6170 |
SABIO-RKi | P50578 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:AKR1A1 Synonyms:ALR1 Publication, ALR1 |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Apical cell membrane By similarity
Cytoplasm and Cytosol
- cytosol By similarity
Cytosol
- cytosol Source: UniProtKB
Plasma Membrane
- apical plasma membrane Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, Cytoplasm, MembranePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedBy similarity | |||
ChainiPRO_0000124619 | 2 – 325 | Aldo-keto reductase family 1 member A1Add BLAST | 324 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineBy similarity | 1 | |
Modified residuei | 4 | PhosphoserineBy similarity | 1 | |
Modified residuei | 127 | N6-acetyllysine; alternateBy similarity | 1 | |
Modified residuei | 127 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 145 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 211 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
PeptideAtlasi | P50578 |
PRIDEi | P50578 |
Expressioni
Gene expression databases
Bgeei | ENSSSCG00000029256, Expressed in adult mammalian kidney and 47 other tissues |
ExpressionAtlasi | P50578, baseline and differential |
Interactioni
Subunit structurei
Monomer.
Protein-protein interaction databases
STRINGi | 9823.ENSSSCP00000020540 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P50578 |
SMRi | P50578 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P50578 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1577, Eukaryota |
HOGENOMi | CLU_023205_0_0_1 |
InParanoidi | P50578 |
TreeFami | TF106492 |
Family and domain databases
CDDi | cd19106, AKR_AKR1A1-4, 1 hit |
Gene3Di | 3.20.20.100, 1 hit |
InterProi | View protein in InterPro IPR020471, AKR IPR044481, AKR1A IPR018170, Aldo/ket_reductase_CS IPR023210, NADP_OxRdtase_dom IPR036812, NADP_OxRdtase_dom_sf |
Pfami | View protein in Pfam PF00248, Aldo_ket_red, 1 hit |
PIRSFi | PIRSF000097, AKR, 1 hit |
PRINTSi | PR00069, ALDKETRDTASE |
SUPFAMi | SSF51430, SSF51430, 1 hit |
PROSITEi | View protein in PROSITE PS00798, ALDOKETO_REDUCTASE_1, 1 hit PS00062, ALDOKETO_REDUCTASE_2, 1 hit PS00063, ALDOKETO_REDUCTASE_3, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALTVG YRHIDCAAIY
60 70 80 90 100
GNELEIGEAL QETVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA
110 120 130 140 150
DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTIRYDATHY KDTWKALEAL
160 170 180 190 200
VAKGLVRALG LSNFSSRQID DVLSVASVRP AVLQVECHPY LAQNELIAHC
210 220 230 240 250
QARGLEVTAY SPLGSSDRAW RDPNEPVLLE EPVVQALAEK YNRSPAQILL
260 270 280 290 300
RWQVQRKVIC IPKSVTPSRI LQNIQVFDFT FSPEEMKQLD ALNKNLRFIV
310 320
PMLTVDGKRV PRDAGHPLYP FNDPY
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 61 | Q → T in AAB60266 (PubMed:7484379). | 1 | |
Sequence conflicti | 271 | L → P in AAB60266 (PubMed:7484379). | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U46064 mRNA Translation: AAB60266.1 AEMK02000049 Genomic DNA No translation available. |
RefSeqi | NP_999055.1, NM_213890.1 |
Genome annotation databases
GeneIDi | 396924 |
KEGGi | ssc:396924 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U46064 mRNA Translation: AAB60266.1 AEMK02000049 Genomic DNA No translation available. |
RefSeqi | NP_999055.1, NM_213890.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AE4 | X-ray | 2.40 | A | 1-325 | [»] | |
1CWN | X-ray | 2.00 | A | 2-325 | [»] | |
1HQT | X-ray | 2.20 | A | 1-325 | [»] | |
3CV7 | X-ray | 2.41 | A | 1-325 | [»] | |
3FX4 | X-ray | 1.99 | A | 1-325 | [»] | |
3H4G | X-ray | 1.85 | A | 1-325 | [»] | |
AlphaFoldDBi | P50578 | |||||
SMRi | P50578 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 9823.ENSSSCP00000020540 |
Chemistry databases
ChEMBLi | CHEMBL4049 |
DrugCentrali | P50578 |
Proteomic databases
PeptideAtlasi | P50578 |
PRIDEi | P50578 |
Genome annotation databases
GeneIDi | 396924 |
KEGGi | ssc:396924 |
Organism-specific databases
CTDi | 10327 |
Phylogenomic databases
eggNOGi | KOG1577, Eukaryota |
HOGENOMi | CLU_023205_0_0_1 |
InParanoidi | P50578 |
TreeFami | TF106492 |
Enzyme and pathway databases
BRENDAi | 1.1.1.2, 6170 |
SABIO-RKi | P50578 |
Miscellaneous databases
EvolutionaryTracei | P50578 |
PROi | PR:P50578 |
Gene expression databases
Bgeei | ENSSSCG00000029256, Expressed in adult mammalian kidney and 47 other tissues |
ExpressionAtlasi | P50578, baseline and differential |
Family and domain databases
CDDi | cd19106, AKR_AKR1A1-4, 1 hit |
Gene3Di | 3.20.20.100, 1 hit |
InterProi | View protein in InterPro IPR020471, AKR IPR044481, AKR1A IPR018170, Aldo/ket_reductase_CS IPR023210, NADP_OxRdtase_dom IPR036812, NADP_OxRdtase_dom_sf |
Pfami | View protein in Pfam PF00248, Aldo_ket_red, 1 hit |
PIRSFi | PIRSF000097, AKR, 1 hit |
PRINTSi | PR00069, ALDKETRDTASE |
SUPFAMi | SSF51430, SSF51430, 1 hit |
PROSITEi | View protein in PROSITE PS00798, ALDOKETO_REDUCTASE_1, 1 hit PS00062, ALDOKETO_REDUCTASE_2, 1 hit PS00063, ALDOKETO_REDUCTASE_3, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | AK1A1_PIG | |
Accessioni | P50578Primary (citable) accession number: P50578 Secondary accession number(s): I3L929 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1996 |
Last sequence update: | February 13, 2019 | |
Last modified: | May 25, 2022 | |
This is version 132 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families