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UniProtKB/Swiss-Prot entry P50578

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AK1A1_PIG
Primary accession number P50578
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 59)
Name and origin of the protein
Protein name Alcohol dehydrogenase [NADP+]
Synonyms EC 1.1.1.2
Aldehyde reductase
Aldo-keto reductase family 1 member A1
Gene name
Name: AKR1A1
Synonyms: ALR, ALR1
From
Sus scrofa (Pig) [TaxID: 9823] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; Sus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7484379 [NCBI, ExPASy, EBI, Israel, Japan]
Flynn T.G., Green N.C., Bhatia M.B., El-Kabbani O.;
"Structure and mechanism of aldehyde reductase.";
Adv. Exp. Med. Biol. 372:193-201(1995).
[2]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1038/nsb0895-687; PubMed=7552731 [NCBI, ExPASy, EBI, Israel, Japan]
el-Kabbani O., Judge K., Ginell S.L., Myles D.A., DeLucas L.J., Flynn T.G.;
"Structure of porcine aldehyde reductase holoenzyme.";
Nat. Struct. Biol. 2:687-692(1995).
[3]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1002/(SICI)1097-0134(199710)29:2<186::AID-PROT6>3.0.CO;2-B; PubMed=9329083 [NCBI, ExPASy, EBI, Israel, Japan]
El-Kabbani O., Carper D.A., McGowan M.H., Devedjiev Y., Rees-Milton K.J., Flynn T.G.;
"Studies on the inhibitor-binding site of porcine aldehyde reductase: crystal structure of the holoenzyme-inhibitor ternary complex.";
Proteins 29:186-192(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U46064; AAB60266.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_999055.1; -.
UniGene Ssc.14521
3D structure databases
PDB
1AE4; X-ray; 2.40 A; A=1-325.[ExPASy / RCSB / EBI]
1CWN; X-ray; 2.00 A; A=1-325.[ExPASy / RCSB / EBI]
1HQT; X-ray; 2.20 A; A=1-325.[ExPASy / RCSB / EBI]
2AO0; X-ray; 1.85 A; A=1-325.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AE4; -.
1CWN; -.
1HQT; -.
2AO0; -.
ModBase P50578.
Ontologies
GO
GO:0008106; Molecular function: alcohol dehydrogenase (NADP+) activity (inferred from electronic annotation from EC).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001395; Aldo/ket_red.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.100; Aldo/ket_red; 1.
PANTHER PTHR11732; Aldo/ket_red; 1.
Pfam PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.
PRINTS PR00069; ALDKETRDTASE.
ProDom PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00798; ALDOKETO_REDUCTASE_1; 1.
PS00062; ALDOKETO_REDUCTASE_2; 1.
PS00063; ALDOKETO_REDUCTASE_3; 1.
Genome annotation databases
GeneID 396924; -.
KEGG ssc:396924; -.
Phylogenomic databases
HOVERGEN P50578; -.
Other
LinkHub P50578; -.
ProtoNet P50578.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; NADP; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   325  324     Alcohol dehydrogenase [NADP+]. PRO_0000124619
NP_BIND   11    20  10     NADP (Potential). 
NP_BIND   211   273  63     NADP. 
ACT_SITE   50    50        Proton donor. 
BINDING   113   113        Substrate. 
SITE   80    80  1     Lowers pKa of active site Tyr (By similarity). 
MOD_RES   2     2        N-acetylalanine (By similarity). 
VARIANT   165   165  1     S -> N. 
STRAND   5     7  3      
STRAND   13    17  5      
TURN   26    28  3      
HELIX   29    38  10      
STRAND   43    45  3      
HELIX   48    50  3      
HELIX   53    60  8      
TURN   61    63  3      
STRAND   64    70  7      
HELIX   72    74  3      
STRAND   76    81  6      
HELIX   83    85  3      
HELIX   88   102  15      
STRAND   107   113  7      
TURN   129   131  3      
HELIX   140   152  13      
STRAND   155   157  3      
STRAND   159   163  5      
HELIX   166   173  8      
STRAND   182   186  5      
HELIX   194   203  10      
STRAND   206   211  6      
HELIX   232   240  9      
HELIX   245   255  11      
TURN   267   269  3      
HELIX   270   274  5      
HELIX   283   290  8      
Sequence information
Length: 325 AA [This is the length of the unprocessed precursor] Molecular weight: 36539 Da [This is the MW of the unprocessed precursor] CRC64: 146F2D1AE8B0A17F [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAIKYALTVG YRHIDCAAIY GNELEIGEAL 

        70         80         90        100        110        120 
TETVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER 

       130        140        150        160        170        180 
GDNPFPKNAD GTIRYDATHY KDTWKALEAL VAKGLVRALG LSNFSSRQID DVLSVASVRP 

       190        200        210        220        230        240 
AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RDPNEPVLLE EPVVQALAEK 

       250        260        270        280        290        300 
YNRSPAQILL RWQVQRKVIC IPKSVTPSRI PQNIQVFDFT FSPEEMKQLD ALNKNLRFIV 

       310        320 
PMLTVDGKRV PRDAGHPLYP FNDPY
P50578 in FASTA format

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