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UniProtKB/Swiss-Prot entry P00327

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

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Entry information
Entry name ADH1E_HORSE
Primary accession number P00327
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 84)
Name and origin of the protein
Protein name Alcohol dehydrogenase E 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 2-375.
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).
[5]
 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
DOI=10.1107/S0907444994005263; PubMed=15299346 [NCBI, ExPASy, EBI, Israel, Japan]
Al-Karadaghi S., Cedergren-Zeppezauer E.S., Hovmoeller S., Petratos K., Terry H., Wilson K.S.;
"Refined crystal structure of liver alcohol dehydrogenase-NADH complex at 1.8-A resolution.";
Acta Crystallogr. D 50:793-807(1994).
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
M64864; AAA30931.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A39872; DEHOAL.
RefSeq NP_001075997.1; -.
UniGene Eca.13382
3D structure databases
PDB
1A71; X-ray; 2.00 A; A/B=1-375.[ExPASy / RCSB / EBI]
1A72; X-ray; 2.60 A; A=2-375.[ExPASy / RCSB / EBI]
1ADB; X-ray; 2.40 A; A/B=1-375.[ExPASy / RCSB / EBI]
1ADC; X-ray; 2.70 A; A/B=1-375.[ExPASy / RCSB / EBI]
1ADF; X-ray; 2.90 A; A=1-375.[ExPASy / RCSB / EBI]
1ADG; X-ray; 2.70 A; A=1-375.[ExPASy / RCSB / EBI]
1AXE; X-ray; 2.00 A; A/B=1-375.[ExPASy / RCSB / EBI]
1AXG; X-ray; 2.50 A; A/B/C/D=1-375.[ExPASy / RCSB / EBI]
1BTO; X-ray; 2.00 A; A/B/C/D=1-375.[ExPASy / RCSB / EBI]
1HET; X-ray; 1.15 A; A/B=1-375.[ExPASy / RCSB / EBI]
1HEU; X-ray; 1.15 A; A/B=1-375.[ExPASy / RCSB / EBI]
1HF3; X-ray; 1.95 A; A/B=1-375.[ExPASy / RCSB / EBI]
1HLD; X-ray; 2.10 A; A/B=1-375.[ExPASy / RCSB / EBI]
1JU9; X-ray; 2.00 A; A/B=1-375.[ExPASy / RCSB / EBI]
1LDE; X-ray; 2.50 A; A/B/C/D=1-375.[ExPASy / RCSB / EBI]
1LDY; X-ray; 2.50 A; A/B/C/D=1-375.[ExPASy / RCSB / EBI]
1MG0; X-ray; 1.80 A; A/B/C/D=1-375.[ExPASy / RCSB / EBI]
1MGO; X-ray; 1.20 A; A/B=1-375.[ExPASy / RCSB / EBI]
1N8K; X-ray; 1.13 A; A/B=1-375.[ExPASy / RCSB / EBI]
1N92; X-ray; 1.47 A; A/B=1-375.[ExPASy / RCSB / EBI]
1P1R; X-ray; 1.57 A; A/B/C/D=1-375.[ExPASy / RCSB / EBI]
1QLH; X-ray; 2.07 A; A=1-375.[ExPASy / RCSB / EBI]
1QLJ; X-ray; 2.80 A; A=1-375.[ExPASy / RCSB / EBI]
1QV6; X-ray; 1.80 A; A/B=1-375.[ExPASy / RCSB / EBI]
1QV7; X-ray; 1.80 A; A/B=1-375.[ExPASy / RCSB / EBI]
1YE3; X-ray; 1.59 A; A=1-375.[ExPASy / RCSB / EBI]
2JHF; X-ray; 1.00 A; A/B=2-375.[ExPASy / RCSB / EBI]
2JHG; X-ray; 1.20 A; A/B=2-375.[ExPASy / RCSB / EBI]
2OHX; X-ray; 1.80 A; A/B=1-375.[ExPASy / RCSB / EBI]
2OXI; X-ray; 2.10 A; A/B=1-375.[ExPASy / RCSB / EBI]
3BTO; X-ray; 1.66 A; A/B/C/D=1-375.[ExPASy / RCSB / EBI]
5ADH; X-ray; 2.90 A; A=1-375.[ExPASy / RCSB / EBI]
6ADH; X-ray; 2.90 A; A/B=1-375.[ExPASy / RCSB / EBI]
7ADH; X-ray; 3.20 A; A=1-375.[ExPASy / RCSB / EBI]
8ADH; X-ray; 2.40 A; A=1-375.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A71; -.
1A72; -.
1ADB; -.
1ADC; -.
1ADF; -.
1ADG; -.
1AXE; -.
1AXG; -.
1BTO; -.
1HET; -.
1HEU; -.
1HF3; -.
1HLD; -.
1JU9; -.
1LDE; -.
1LDY; -.
1MG0; -.
1MGO; -.
1N8K; -.
1N92; -.
1P1R; -.
1QLH; -.
1QLJ; -.
1QV6; -.
1QV7; -.
1YE3; -.
2JHF; -.
2JHG; -.
2OHX; -.
2OXI; -.
3BTO; -.
5ADH; -.
6ADH; -.
7ADH; -.
8ADH; -.
ModBase P00327.
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.
Genome annotation databases
GeneID 100034242; -.
Phylogenomic databases
HOVERGEN P00327; -.
Other
DrugBank DB01093; Dimethyl sulfoxide.
LinkHub P00327; -.
ProtoNet P00327.
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   375  374     Alcohol dehydrogenase E chain. PRO_0000160656
NP_BIND   200   205  6     NAD. 
NP_BIND   293   295  3     NAD. 
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   175   175        Zinc 1; catalytic. 
BINDING   224   224        NAD. 
BINDING   229   229        NAD. 
BINDING   370   370        NAD. 
MOD_RES   2     2        N-acetylserine. 
STRAND   8    15  8      
STRAND   23    29  7      
STRAND   36    45  10      
HELIX   48    54  7      
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   116   119  4      
STRAND   130   133  4      
STRAND   136   139  4      
TURN   142   144  3      
STRAND   147   154  8      
HELIX   155   157  3      
STRAND   158   160  3      
HELIX   167   170  4      
HELIX   171   174  4      
HELIX   176   185  10      
TURN   186   188  3      
STRAND   195   199  5      
HELIX   203   214  12      
STRAND   218   223  6      
HELIX   227   229  3      
HELIX   230   236  7      
STRAND   239   242  4      
HELIX   244   246  3      
HELIX   251   258  8      
STRAND   263   268  6      
HELIX   273   282  10      
TURN   285   287  3      
STRAND   289   292  4      
STRAND   302   304  3      
HELIX   307   310  4      
STRAND   314   317  4      
HELIX   320   322  3      
HELIX   325   337  13      
HELIX   344   346  3      
STRAND   347   352  6      
HELIX   353   355  3      
HELIX   356   364  9      
STRAND   369   374  6      
Sequence information
Length: 375 AA [This is the length of the unprocessed precursor] Molecular weight: 39936 Da [This is the MW of the unprocessed precursor] CRC64: DA701D2F6AB69C9D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWEEKK PFSIEEVEVA PPKAHEVRIK MVATGICRSD DHVVSGTLVT 

        70         80         90        100        110        120 
PLPVIAGHEA AGIVESIGEG VTTVRPGDKV IPLFTPQCGK CRVCKHPEGN FCLKNDLSMP 

       130        140        150        160        170        180 
RGTMQDGTSR FTCRGKPIHH FLGTSTFSQY TVVDEISVAK IDAASPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGSAVKVAKV TQGSTCAVFG LGGVGLSVIM GCKAAGAARI IGVDINKDKF AKAKEVGATE 

       250        260        270        280        290        300 
CVNPQDYKKP IQEVLTEMSN GGVDFSFEVI GRLDTMVTAL SCCQEAYGVS VIVGVPPDSQ 

       310        320        330        340        350        360 
NLSMNPMLLL SGRTWKGAIF GGFKSKDSVP KLVADFMAKK FALDPLITHV LPFEKINEGF 

       370 
DLLRSGESIR TILTF
P00327 in FASTA format

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