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Protein

Alcohol dehydrogenase [NADP(+)]

Gene

AKR1A1

Organism
Sus scrofa (Pig)
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).By similarity

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei45NADPBy similarity1
Active sitei50Proton donor1 Publication1
Sitei80Lowers pKa of active site TyrBy similarity1
Binding sitei113Substrate1 Publication1
Binding sitei184NADPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 20NADPSequence analysis10
Nucleotide bindingi21 – 23NADPBy similarity3
Nucleotide bindingi162 – 163NADPBy similarity2
Nucleotide bindingi211 – 273NADP1 PublicationAdd BLAST63

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14995.
BRENDAi1.1.1.2. 6170.
SABIO-RKP50578.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase [NADP(+)] (EC:1.1.1.2)
Alternative name(s):
Aldehyde reductase
Aldo-keto reductase family 1 member A1
Gene namesi
Name:AKR1A1
Synonyms:ALR, ALR1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4049.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001246192 – 325Alcohol dehydrogenase [NADP(+)]Add BLAST324

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei4PhosphoserineBy similarity1
Modified residuei127N6-acetyllysine; alternateBy similarity1
Modified residuei127N6-succinyllysine; alternateBy similarity1
Modified residuei145N6-succinyllysineBy similarity1
Modified residuei211PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PeptideAtlasiP50578.
PRIDEiP50578.

Interactioni

Subunit structurei

Monomer.

Chemistry databases

BindingDBiP50578.

Structurei

Secondary structure

1325
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Beta strandi13 – 17Combined sources5
Turni26 – 28Combined sources3
Helixi29 – 38Combined sources10
Beta strandi43 – 45Combined sources3
Helixi48 – 50Combined sources3
Helixi53 – 63Combined sources11
Beta strandi68 – 70Combined sources3
Helixi72 – 74Combined sources3
Beta strandi76 – 81Combined sources6
Helixi83 – 85Combined sources3
Helixi88 – 102Combined sources15
Beta strandi107 – 113Combined sources7
Beta strandi115 – 118Combined sources4
Beta strandi120 – 122Combined sources3
Beta strandi131 – 133Combined sources3
Helixi140 – 152Combined sources13
Beta strandi155 – 163Combined sources9
Helixi166 – 173Combined sources8
Beta strandi182 – 186Combined sources5
Helixi194 – 203Combined sources10
Beta strandi206 – 211Combined sources6
Turni212 – 217Combined sources6
Helixi228 – 230Combined sources3
Helixi232 – 241Combined sources10
Helixi245 – 255Combined sources11
Helixi267 – 274Combined sources8
Helixi283 – 290Combined sources8
Beta strandi302 – 305Combined sources4
Beta strandi311 – 313Combined sources3
Helixi320 – 322Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AE4X-ray2.40A1-325[»]
1CWNX-ray2.00A2-325[»]
1HQTX-ray2.20A1-325[»]
3CV7X-ray2.41A1-325[»]
3FX4X-ray1.99A1-325[»]
3H4GX-ray1.85A1-325[»]
ProteinModelPortaliP50578.
SMRiP50578.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50578.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldo/keto reductase family.Curated

Phylogenomic databases

HOVERGENiHBG000020.
InParanoidiP50578.
KOiK00002.

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.

P50578-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALTVG YRHIDCAAIY
60 70 80 90 100
GNELEIGEAL TETVGPGKAV 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 PQNIQVFDFT FSPEEMKQLD ALNKNLRFIV
310 320
PMLTVDGKRV PRDAGHPLYP FNDPY
Length:325
Mass (Da):36,539
Last modified:January 23, 2007 - v2
Checksum:i146F2D1AE8B0A17F
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti165S → N.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U46064 mRNA. Translation: AAB60266.1.
RefSeqiNP_999055.1. NM_213890.1.
UniGeneiSsc.14521.

Genome annotation databases

GeneIDi396924.
KEGGissc:396924.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U46064 mRNA. Translation: AAB60266.1.
RefSeqiNP_999055.1. NM_213890.1.
UniGeneiSsc.14521.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AE4X-ray2.40A1-325[»]
1CWNX-ray2.00A2-325[»]
1HQTX-ray2.20A1-325[»]
3CV7X-ray2.41A1-325[»]
3FX4X-ray1.99A1-325[»]
3H4GX-ray1.85A1-325[»]
ProteinModelPortaliP50578.
SMRiP50578.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP50578.
ChEMBLiCHEMBL4049.

Proteomic databases

PeptideAtlasiP50578.
PRIDEiP50578.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396924.
KEGGissc:396924.

Organism-specific databases

CTDi10327.

Phylogenomic databases

HOVERGENiHBG000020.
InParanoidiP50578.
KOiK00002.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14995.
BRENDAi1.1.1.2. 6170.
SABIO-RKP50578.

Miscellaneous databases

EvolutionaryTraceiP50578.
PROiP50578.

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_PIG
AccessioniPrimary (citable) accession number: P50578
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 110 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.