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Protein

Alcohol dehydrogenase [NADP(+)]

Gene

Akr1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols. Catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Has broad substrate specificity. 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). Catalyzes the NADPH-dependent reduction of 3-deoxyglucosone (3-DG).By similarity

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei50Proton donorBy similarity1
Sitei80Lowers pKa of active site TyrBy similarity1
Binding sitei113SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 20NADPSequence analysis10
Nucleotide bindingi211 – 273NADPBy similarityAdd BLAST63

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiR-RNO-156590. Glutathione conjugation.
R-RNO-5661270. Catabolism of glucuronate to xylulose-5-phosphate.
SABIO-RKP51635.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase [NADP(+)] (EC:1.1.1.2)
Alternative name(s):
3-DG-reducing enzyme
Aldehyde reductase
Aldo-keto reductase family 1 member A1
Gene namesi
Name:Akr1a1
Synonyms:Alr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi68346. Akr1a1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3871.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001246202 – 325Alcohol dehydrogenase [NADP(+)]Add BLAST324

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonine1 Publication1
Modified residuei4PhosphoserineCombined sources1
Glycosylationi23N-linked (Glc) (glycation)1
Modified residuei38PhosphoserineBy similarity1
Glycosylationi68N-linked (Glc) (glycation)1
Glycosylationi85N-linked (Glc) (glycation)1
Modified residuei127N6-acetyllysine; alternateBy similarity1
Modified residuei127N6-succinyllysine; alternateBy similarity1
Glycosylationi141N-linked (Glc) (glycation)1
Modified residuei145N6-succinyllysineBy similarity1
Glycosylationi153N-linked (Glc) (glycation)1
Modified residuei211PhosphoserineBy similarity1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei13Not glycated1
Sitei30Not glycated1
Sitei34Not glycated1
Sitei61Not glycated1
Sitei80Not glycated1
Sitei97Not glycated1
Sitei127Not glycated1
Sitei134Not glycated1
Sitei145Not glycated1
Sitei157Not glycated1
Sitei240Not glycated1
Sitei257Not glycated1
Sitei263Not glycated1
Sitei287Not glycated1
Sitei294Not glycated1
Sitei308Not glycated1

Keywords - PTMi

Acetylation, Glycation, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP51635.
PRIDEiP51635.

2D gel databases

World-2DPAGE0004:P51635.

PTM databases

iPTMnetiP51635.
PhosphoSitePlusiP51635.

Expressioni

Gene expression databases

BgeeiENSRNOG00000016727.
GenevisibleiP51635. RN.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

MINTiMINT-4564842.
STRINGi10116.ENSRNOP00000023072.

Chemistry databases

BindingDBiP51635.

Structurei

3D structure databases

ProteinModelPortaliP51635.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP51635.
KOiK00002.
OMAiWDALEKI.
OrthoDBiEOG091G0D69.
PhylomeDBiP51635.
TreeFamiTF106492.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51635-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTASSVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALSVG YRHIDCASVY
60 70 80 90 100
GNETEIGEAL KESVGAGKAV PREELFVTSK LWNTKHHPED VEPAVRKTLA
110 120 130 140 150
DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTVKYDSTHY KETWKALEAL
160 170 180 190 200
VAKGLVKALG LSNFSSRQID DVLSVASVRP AVLQVECHPY LAQNELIAHC
210 220 230 240 250
QARGLEVTAY SPLGSSDRAW RHPDEPVLLE EPVVLALAEK HGRSPAQILL
260 270 280 290 300
RWQVQRKVIC IPKSITPSRI LQNIQVFDFT FSPEEMKQLD ALNKNWRYIV
310 320
PMITVDGKRV PRDAGHPLYP FNDPY
Length:325
Mass (Da):36,506
Last modified:January 23, 2007 - v2
Checksum:iF95573B7411884DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10854 mRNA. Translation: BAA01627.1.
BC059133 mRNA. Translation: AAH59133.1.
PIRiJN0629.
RefSeqiNP_112262.1. NM_031000.3.
UniGeneiRn.835.

Genome annotation databases

EnsembliENSRNOT00000023072; ENSRNOP00000023072; ENSRNOG00000016727.
GeneIDi78959.
KEGGirno:78959.
UCSCiRGD:68346. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10854 mRNA. Translation: BAA01627.1.
BC059133 mRNA. Translation: AAH59133.1.
PIRiJN0629.
RefSeqiNP_112262.1. NM_031000.3.
UniGeneiRn.835.

3D structure databases

ProteinModelPortaliP51635.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4564842.
STRINGi10116.ENSRNOP00000023072.

Chemistry databases

BindingDBiP51635.
ChEMBLiCHEMBL3871.

PTM databases

iPTMnetiP51635.
PhosphoSitePlusiP51635.

2D gel databases

World-2DPAGE0004:P51635.

Proteomic databases

PaxDbiP51635.
PRIDEiP51635.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023072; ENSRNOP00000023072; ENSRNOG00000016727.
GeneIDi78959.
KEGGirno:78959.
UCSCiRGD:68346. rat.

Organism-specific databases

CTDi10327.
RGDi68346. Akr1a1.

Phylogenomic databases

eggNOGiKOG1577. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00760000119041.
HOGENOMiHOG000250272.
HOVERGENiHBG000020.
InParanoidiP51635.
KOiK00002.
OMAiWDALEKI.
OrthoDBiEOG091G0D69.
PhylomeDBiP51635.
TreeFamiTF106492.

Enzyme and pathway databases

ReactomeiR-RNO-156590. Glutathione conjugation.
R-RNO-5661270. Catabolism of glucuronate to xylulose-5-phosphate.
SABIO-RKP51635.

Miscellaneous databases

PROiP51635.

Gene expression databases

BgeeiENSRNOG00000016727.
GenevisibleiP51635. RN.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 2 hits.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PIRSFiPIRSF000097. AKR. 1 hit.
PRINTSiPR00069. ALDKETRDTASE.
SUPFAMiSSF51430. SSF51430. 1 hit.
PROSITEiPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAK1A1_RAT
AccessioniPrimary (citable) accession number: P51635
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.