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Reviewed, UniProtKB/Swiss-Prot P49645 (ADH1_APTAU)

Last modified June 16, 2009. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

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Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase 1
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase I
Gene names
Name: ADH1
OrganismApteryx australis (Brown kiwi)
Taxonomic identifier8822 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Palaeognathae › Apterygiformes › Apterygidae › Apteryx

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Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

An alcohol + NAD+ = an aldehyde or ketone + NADH.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family. Class-I subfamily.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalcohol dehydrogenase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 375374Alcohol dehydrogenase 1
PRO_0000160671

Regions

Nucleotide binding200 – 2056NAD By similarity
Nucleotide binding293 – 2953NAD By similarity

Sites

Metal binding471Zinc 1; catalytic By similarity
Metal binding681Zinc 1; catalytic By similarity
Metal binding981Zinc 2 By similarity
Metal binding1011Zinc 2 By similarity
Metal binding1041Zinc 2 By similarity
Metal binding1121Zinc 2 By similarity
Metal binding1751Zinc 1; catalytic By similarity
Binding site2241NAD By similarity
Binding site2291NAD By similarity
Binding site3701NAD By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P49645-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A6EBC1BEB0D66E02

FASTA37539,631
        10         20         30         40         50         60 
MSTAGKVIKC KAAVLWEPKK PFSIEEVEVA PPKAHEVRIK ILATGICRSD DHVITGALVR 

        70         80         90        100        110        120 
PFPIILGHEA AGVVESVGEG VTSVKPGDKV IPLFVPQCGE CSACLSTKGN LCSKNDIGSA 

       130        140        150        160        170        180 
SGLMPDGTTR FTCKGKAIHH FIGTSTFTEY TVVHETAVAK IAAAAPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGAAVQTAKV EPGSTCAVFG LGGVGLSVVM GCKAAGASRI IAIDINKDKF AKAKELGATD 

       250        260        270        280        290        300 
CVNPKDFTKP IHEVLMEMTG LGVDYSFEVI GHTETMAAAL ASCHFNYGVS VILGVPPAAE 

       310        320        330        340        350        360 
KISFDPMLLF SGRTWKGSVF GGWKSKDAVP KLVADYMEKK FVLEPLITHT LPFIKINEGF 

       370 
DLLRKGKSIR SVLVF

« Hide

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References

[1]"Alcohol dehydrogenase of class I: kiwi liver enzyme, parallel evolution in separate vertebrate lines, and correlation with 12S rRNA patterns."
Hjelmqvist L., Metsis M., Persson H., Hoeoeg J.-O., McLennan J., Joernvall H.
FEBS Lett. 367:306-310(1995) [PubMed: 7541757] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Multiplicity of N-terminal structures of medium-chain alcohol dehydrogenases. Mass-spectrometric analysis of plant, lower vertebrate and higher vertebrate class I, II, and III forms of the enzyme."
Hjelmqvist L., Hackett M., Shafqat J., Danielsson O., Iida J., Hendrickson R.C., Michel H., Shabanowitz J., Hunt D.F., Joernvall H.
FEBS Lett. 367:237-240(1995) [PubMed: 7607314] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, ACETYLATION AT SER-2.

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Cross-references

Sequence databases

S78778 mRNA. Translation: AAC60755.2.
PIRS66272.

3D structure databases

HSSPHSSP built from PDB template 1HT0 based on UniProtKB P00326.
SMRP49645. Positions 2-375.
ModBaseSearch...

Phylogenomic databases

HOVERGENP49645.

Enzyme and pathway databases

BRENDA1.1.1.1. 302181.

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...

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Entry information

Entry nameADH1_APTAU
AccessionPrimary (citable) accession number: P49645
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 56 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

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