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Reviewed, UniProtKB/Swiss-Prot P14941 (ADH_THEBR)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    NADP-dependent alcohol dehydrogenase
    EC=1.1.1.2
Gene names
Name: adh
OrganismThermoanaerobacter brockii (Thermoanaerobium brockii)
Taxonomic identifier29323 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteriaceaeThermoanaerobacter

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

An alcohol + NADP+ = an aldehyde + NADPH.

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Homotetramer.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Ontologies

Keywords
   LigandMetal-binding
NADP
Zinc
   Molecular functionOxidoreductase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionalcohol dehydrogenase (NADP+) activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352NADP-dependent alcohol dehydrogenase
PRO_0000160749

Sites

Metal binding371Zinc; catalytic
Metal binding591Zinc; catalytic
Metal binding1501Zinc; catalytic

Secondary structure

................................................................... 352
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14941-1 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: E124A5351AD55185

FASTA35237,647
        10         20         30         40         50         60 
MKGFAMLSIG KVGWIEKEKP APGPFDAIVR PLAVAPCTSD IHTVFEGAIG ERHNMILGHE 

        70         80         90        100        110        120 
AVGEVVEVGS EVKDFKPGDR VVVPAITPDW RTSEVQRGYH QHSGGMLAGW KFSNVKDGVF 

       130        140        150        160        170        180 
GEFFHVNDAD MNLAHLPKEI PLEAAVMIPD MMTTGFHGAE LADIELGATV AVLGIGPVGL 

       190        200        210        220        230        240 
MAVAGAKLRG AGRIIAVGSR PVCVDAAKYY GATDIVNYKD GPIESQIMNL TEGKGVDAAI 

       250        260        270        280        290        300 
IAGGNADIMA TAVKIVKPGG TIANVNYFGE GEVLPVPRLE WGCGMAHKTI KGGLCPGGRL 

       310        320        330        340        350 
RMERLIDLVF YKRVDPSKLV THVFRGFDNI EKAFMLMKDK PKDLIKPVVI LA 

« Hide

References

[1]"Amino acid sequence of alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii."
Peretz M., Burstein Y.
Biochemistry 28:6549-6555(1989) [PubMed: 2790012] [Abstract]
Cited for: PROTEIN SEQUENCE.
Strain: ATCC 53556 / HTD4 / DSM 1457.
[2]Burstein Y.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 53556 / HTD4 / DSM 1457.
[3]"NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii."
Korkhin Y., Kalb A.J., Peretz M., Bogin O., Burstein Y., Frolow F.
J. Mol. Biol. 278:967-981(1998) [PubMed: 9836873] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

X64841 Genomic DNA. Translation: CAA46053.1.
PIRA32973.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1BXZX-ray2.99A/B/C/D1-352[»]
1YKFX-ray2.50A/B/C/D1-352[»]
2NVBX-ray2.80A/B/C/D1-352[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.1.1.2. 140632.

Family and domain databases

InterProIPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
[Graphical view]
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH_THEBR
AccessionPrimary (citable) accession number: P14941
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents