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UniProtKB/Swiss-Prot entry P25984

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

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Entry information
Entry name ADH_CLOBE
Primary accession number P25984
Secondary accession number Q9R559
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on December 4, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 64)
Name and origin of the protein
Protein name NADP-dependent alcohol dehydrogenase
Synonyms EC 1.1.1.2
CbADH
Gene name
Name: adh
From
Clostridium beijerinckii (Clostridium MP) [TaxID: 1520] 
Taxonomy Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; Clostridium.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NRRL B-593;
Rifaat M.M., Chen J.S.;
"Cloning and sequence analysis of a gene encoding a medium-chain zinc-containing alcohol dehydrogenase from the Gram-positive anaerobe Clostridium beijerinckii NRRL B593.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[2]
 PROTEIN SEQUENCE OF 1-21.
STRAIN=NESTE 255, and NRRL B-593;
PubMed=8349550 [NCBI, ExPASy, EBI, Israel, Japan]
Ismaiel A.A., Zhu C.X., Colby G.D., Chen J.S.;
"Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii.";
J. Bacteriol. 175:5097-5105(1993).
[3]
 X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
DOI=10.1006/jmbi.1998.1750; PubMed=9836873 [NCBI, ExPASy, EBI, Israel, Japan]
Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F.;
"NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii.";
J. Mol. Biol. 278:967-981(1998).
[4]
 X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS).
DOI=10.1110/ps.0222102; PubMed=12381840 [NCBI, ExPASy, EBI, Israel, Japan]
Bogin O., Levin I., Hacham Y., Tel-Or S., Peretz M., Frolow F., Burstein Y.;
"Structural basis for the enhanced thermal stability of alcohol dehydrogenase mutants from the mesophilic bacterium Clostridium beijerinckii: contribution of salt bridging.";
Protein Sci. 11:2561-2574(2002).
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
AF157307; AAA23199.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
3D structure databases
PDB
1JQB; X-ray; 1.97 A; A/B/C/D=1-351.[ExPASy / RCSB / EBI]
1KEV; X-ray; 2.05 A; A/B/C/D=1-351.[ExPASy / RCSB / EBI]
1PED; X-ray; 2.15 A; A/B/C/D=1-351.[ExPASy / RCSB / EBI]
2B83; X-ray; 2.25 A; A/B/C/D=1-351.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1JQB; -.
1KEV; -.
1PED; -.
2B83; -.
ModBase P25984.
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 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.
BLOCKS P25984.
ProtoNet P25984.
Other
LinkHub P25984; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Metal-binding; NADP; Oxidoreductase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   351  351     NADP-dependent alcohol dehydrogenase. PRO_0000160739
METAL   37    37        Zinc; catalytic. 
METAL   59    59        Zinc; catalytic. 
METAL   60    60        Zinc; catalytic. 
METAL   150   150        Zinc; catalytic. 
STRAND   2     8  7      
STRAND   11    16  6      
STRAND   27    34  8      
HELIX   38    46  9      
STRAND   53    56  4      
STRAND   61    68  8      
STRAND   80    83  4      
STRAND   90    92  3      
HELIX   93    96  4      
HELIX   100   102  3      
TURN   106   109  4      
TURN   113   115  3      
STRAND   119   128  10      
HELIX   129   132  4      
HELIX   142   146  5      
TURN   147   150  4      
HELIX   151   161  11      
STRAND   170   173  4      
HELIX   177   187  11      
TURN   188   190  3      
STRAND   194   197  4      
HELIX   201   210  10      
STRAND   213   216  4      
HELIX   218   220  3      
HELIX   223   230  8      
TURN   231   233  3      
STRAND   236   241  6      
HELIX   248   255  8      
STRAND   256   264  9      
STRAND   270   277  8      
TURN   278   281  4      
HELIX   282   284  3      
STRAND   289   293  5      
HELIX   298   310  13      
HELIX   316   319  4      
STRAND   320   326  7      
HELIX   327   329  3      
HELIX   330   339  10      
STRAND   345   350  6      
Sequence information
Length: 351 AA [This is the length of the unprocessed precursor] Molecular weight: 37716 Da [This is the MW of the unprocessed precursor] CRC64: E1E925D37D7513B7 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MKGFAMLGIN KLGWIEKERP VAGSYDAIVR PLAVSPCTSD IHTVFEGALG DRKNMILGHE 

        70         80         90        100        110        120 
AVGEVVEVGS EVKDFKPGDR VIVPCTTPDW RSLEVQAGFQ QHSNGMLAGW KFSNFKDGVF 

       130        140        150        160        170        180 
GEYFHVNDAD MNLAILPKDM PLENAVMITD MMTTGFHGAE LADIQMGSSV VVIGIGAVGL 

       190        200        210        220        230        240 
MGIAGAKLRG AGRIIGVGSR PICVEAAKFY GATDILNYKN GHIVDQVMKL TNGKGVDRVI 

       250        260        270        280        290        300 
MAGGGSETLS QAVSMVKPGG IISNINYHGS GDALLIPRVE WGCGMAHKTI KGGLCPGGRL 

       310        320        330        340        350 
RAEMLRDMVV YNRVDLSKLV THVYHGFDHI EEALLLMKDK PKDLIKAVVI L
P25984 in FASTA format

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