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UniProtKB/Swiss-Prot entry P00328

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

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Entry information
Entry name ADH1S_HORSE
Primary accession number P00328
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 79)
Name and origin of the protein
Protein name Alcohol dehydrogenase S chain
Synonym EC 1.1.1.1
Gene name None
From
Equus caballus (Horse) [TaxID: 9796] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1712777 [NCBI, ExPASy, EBI, Israel, Japan]
Park D.H., Plapp B.V.;
"Isoenzymes of horse liver alcohol dehydrogenase active on ethanol and steroids. cDNA cloning, expression, and comparison of active sites.";
J. Biol. Chem. 266:13296-13302(1991).
[2]
 PROTEIN SEQUENCE OF 2-374.
TISSUE=Liver;
DOI=10.1111/j.1432-1033.1970.tb01050.x; PubMed=5466062 [NCBI, ExPASy, EBI, Israel, Japan]
Joernvall H.;
"Horse liver alcohol dehydrogenase. On the primary structures of the isoenzymes.";
Eur. J. Biochem. 16:41-49(1970).
[3]
 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
DOI=10.1016/0022-2836(76)90072-3; PubMed=178875 [NCBI, ExPASy, EBI, Israel, Japan]
Eklund H., Nordstroem B., Zeppezauer E., Soederlund G., Ohlsson I., Boiwe T., Soederberg B.-O., Tapia O., Braenden C.-I., Aakeson A.;
"Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4-A resolution.";
J. Mol. Biol. 102:27-59(1976).
[4]
 X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
DOI=10.1021/bi00320a014; PubMed=6098306 [NCBI, ExPASy, EBI, Israel, Japan]
Eklund H., Samama J.-P., Jones T.A.;
"Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase.";
Biochemistry 23:5982-5996(1984).
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
M64865; AAA30932.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B39872; DEHOAS.
RefSeq NP_001075414.1; -.
UniGene Eca.13101
3D structure databases
PDB
1EE2; X-ray; 1.54 A; A/B=1-374.[ExPASy / RCSB / EBI]
PDBsum 1EE2; -.
ModBase P00328.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004022; Molecular function: alcohol dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR013154; AlcDHase_GroES-like.
IPR002085; AlcDHase_SF_Zn.
IPR013149; AlcDHase_Zn-bd.
IPR002328; AlcDHase_Zn_CS.
Graphical view of domain structure.
PANTHER PTHR11695; ADH_Sf_Zn; 1.
Pfam PF08240; ADH_N; 1.
PF00107; ADH_zinc_N; 1.
Pfam graphical view of domain structure.
PROSITE PS00059; ADH_ZINC; 1.
ProtoNet P00328.
Other
SWISS-3DIMAGE P00328.
Genome annotation databases
GeneID 100034175; -.
Phylogenomic databases
HOVERGEN P00328; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   374  373     Alcohol dehydrogenase S chain. PRO_0000160657
METAL   47    47        Zinc 1; catalytic. 
METAL   68    68        Zinc 1; catalytic. 
METAL   98    98        Zinc 2. 
METAL   101   101        Zinc 2. 
METAL   104   104        Zinc 2. 
METAL   112   112        Zinc 2. 
METAL   174   174        Zinc 1; catalytic. 
MOD_RES   2     2        N-acetylserine. 
CONFLICT   44    44        A -> T (in Ref. 2; AA sequence). 
CONFLICT   60    60        A -> T (in Ref. 2; AA sequence). 
CONFLICT   116   116        L -> SL (in Ref. 2; AA sequence). 
CONFLICT   172   172        V -> I (in Ref. 2; AA sequence). 
CONFLICT   277   277        A -> T (in Ref. 2; AA sequence). 
STRAND   8    15  8      
STRAND   23    29  7      
STRAND   36    45  10      
HELIX   48    55  8      
STRAND   56    58  3      
STRAND   62    65  4      
STRAND   69    77  9      
STRAND   89    92  4      
STRAND   99   101  3      
HELIX   102   105  4      
STRAND   106   108  3      
STRAND   129   132  4      
STRAND   135   138  4      
TURN   141   143  3      
STRAND   146   153  8      
HELIX   154   156  3      
STRAND   157   159  3      
HELIX   166   169  4      
HELIX   170   173  4      
HELIX   175   184  10      
TURN   185   187  3      
STRAND   194   198  5      
HELIX   202   213  12      
STRAND   217   222  6      
HELIX   226   228  3      
HELIX   229   234  6      
STRAND   238   241  4      
HELIX   243   245  3      
HELIX   250   257  8      
STRAND   262   267  6      
HELIX   272   281  10      
TURN   284   286  3      
STRAND   288   291  4      
STRAND   301   303  3      
HELIX   306   309  4      
STRAND   313   316  4      
HELIX   319   321  3      
HELIX   324   336  13      
HELIX   343   345  3      
STRAND   346   351  6      
HELIX   352   354  3      
HELIX   355   363  9      
STRAND   368   373  6      
Sequence information
Length: 374 AA [This is the length of the unprocessed precursor] Molecular weight: 39623 Da [This is the MW of the unprocessed precursor] CRC64: 2B15710A038DA013 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWEQKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD DHVVSGTLVA 

        70         80         90        100        110        120 
PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFIPQCGK CSVCKHPEGN LCLKNLSMPR 

       130        140        150        160        170        180 
GTMQDGTSRF TCRGKPIHHF LGTSTFSQYT VVDEISVAKI DAASPLEKVC LVGCGFSTGY 

       190        200        210        220        230        240 
GSAVKVAKVT QGSTCAVFGL GGVGLSVIMG CKAAGAARII GVDINKDKFA KAKEVGATEC 

       250        260        270        280        290        300 
VNPQDYKKPI QEVLTEMSNG GVDFSFEVIG RLDTMVAALS CCQEAYGVSV IVGVPPDSQN 

       310        320        330        340        350        360 
LSMNPMLLLS GRTWKGAIFG GFKSKDSVPK LVADFMAKKF ALDPLITHVL PFEKINEGFD 

       370 
LLRSGKSIRT ILTF
P00328 in FASTA format

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