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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451NADPBy similarity
Active sitei50 – 501Proton donor1 Publication
Sitei80 – 801Lowers pKa of active site TyrBy similarity
Binding sitei113 – 1131Substrate1 Publication
Binding sitei184 – 1841NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 2010NADPSequence analysis
Nucleotide bindingi21 – 233NADPBy similarity
Nucleotide bindingi162 – 1632NADPBy similarity
Nucleotide bindingi211 – 27363NADP1 PublicationAdd
BLAST

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

ChEMBLiCHEMBL4049.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 325324Alcohol dehydrogenase [NADP(+)]PRO_0000124619Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei127 – 1271N6-acetyllysine; alternateBy similarity
Modified residuei127 – 1271N6-succinyllysine; alternateBy similarity
Modified residuei145 – 1451N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PRIDEiP50578.

Interactioni

Subunit structurei

Monomer.

Chemistry

BindingDBiP50578.

Structurei

Secondary structure

1
325
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi13 – 175Combined sources
Turni26 – 283Combined sources
Helixi29 – 3810Combined sources
Beta strandi43 – 453Combined sources
Helixi48 – 503Combined sources
Helixi53 – 6311Combined sources
Beta strandi68 – 703Combined sources
Helixi72 – 743Combined sources
Beta strandi76 – 816Combined sources
Helixi83 – 853Combined sources
Helixi88 – 10215Combined sources
Beta strandi107 – 1137Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi120 – 1223Combined sources
Beta strandi131 – 1333Combined sources
Helixi140 – 15213Combined sources
Beta strandi155 – 1639Combined sources
Helixi166 – 1738Combined sources
Beta strandi182 – 1865Combined sources
Helixi194 – 20310Combined sources
Beta strandi206 – 2116Combined sources
Turni212 – 2176Combined sources
Helixi228 – 2303Combined sources
Helixi232 – 24110Combined sources
Helixi245 – 25511Combined sources
Helixi267 – 2748Combined sources
Helixi283 – 2908Combined sources
Beta strandi302 – 3054Combined sources
Beta strandi311 – 3133Combined sources
Helixi320 – 3223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-325.
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

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti165 – 1651S → N.

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
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. Positions 2-325.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP50578.
ChEMBLiCHEMBL4049.

Proteomic databases

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.

Family and domain databases

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...

Publicationsi

  1. "Structure and mechanism of aldehyde reductase."
    Flynn T.G., Green N.C., Bhatia M.B., El-Kabbani O.
    Adv. Exp. Med. Biol. 372:193-201(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  3. "Studies on the inhibitor-binding site of porcine aldehyde reductase: crystal structure of the holoenzyme-inhibitor ternary complex."
    El-Kabbani O., Carper D.A., McGowan M.H., Devedjiev Y., Rees-Milton K.J., Flynn T.G.
    Proteins 29:186-192(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

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: December 9, 2015
This is version 105 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.