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Reviewed, UniProtKB/Swiss-Prot P80338 (ADH1_STRCA)

Last modified June 16, 2009. Version 54. 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
OrganismStruthio camelus (Ostrich)
Taxonomic identifier8801 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Palaeognathae › Struthioniformes › Struthionidae › Struthio

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Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Chain1 – 374374Alcohol dehydrogenase 1
PRO_0000160674

Regions

Nucleotide binding199 – 2046NAD By similarity
Nucleotide binding292 – 2943NAD By similarity

Sites

Metal binding461Zinc 1; catalytic By similarity
Metal binding671Zinc 1; catalytic By similarity
Metal binding971Zinc 2 By similarity
Metal binding1001Zinc 2 By similarity
Metal binding1031Zinc 2 By similarity
Metal binding1111Zinc 2 By similarity
Metal binding1741Zinc 1; catalytic By similarity
Binding site2231NAD By similarity
Binding site2281NAD By similarity
Binding site3691NAD By similarity

Amino acid modifications

Modified residue11N-acetylserine Ref.2 Ref.3

Natural variations

Natural variant1121R → C

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Sequences

Sequence LengthMass (Da)Tools
P80338-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 3ACC5386332EEC3C

FASTA37439,583
        10         20         30         40         50         60 
STAGKVIKCK AAVLWEPKKP FSIEEVEVAP PKAHEVRVKI IATGICRSDD HVISGVLVMP 

        70         80         90        100        110        120 
FPIILGHEAA GVVESVGEGV TSVKPGDKVI PLFVPQCGEC SVCLSTKGNL CRKNDIGPAS 

       130        140        150        160        170        180 
ALMPDGTSRF TCKGKAIHHF AGTSTFTEYT VLHETAVAKI DAAAPLEKVC LIGCGFSTGY 

       190        200        210        220        230        240 
GAALQTAKVE PGSTCAVFGL GGVGLSVVMG CKAAGASRII GVDINKDKFA KAKELGATDC 

       250        260        270        280        290        300 
VNPKDFTKPI HEVLMEMTGL GVDYSFEVIG HTETMAAALA SCHFNYGVSV IVGVPPAAEK 

       310        320        330        340        350        360 
LSFDPMLLFS GRTWKGSVFG GWKSKDSVPK LVADYMEKKF VLDPLITHTL PFHKINEGFD 

       370 
LLRTGKSIRS VLLF

« Hide

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References

[1]"Diversity of vertebrate class I alcohol dehydrogenase. Mammalian and non-mammalian enzyme functions correlated through the structure of a ratite enzyme."
Estonius M., Hjelmqvist L., Joernvall H.
Eur. J. Biochem. 224:373-378(1994) [PubMed: 7925350] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Alcoholytic deblocking of N-terminally acetylated peptides and proteins for sequence analysis."
Bergman T., Gheorghe M.T., Hjelmqvist L., Joernvall H.
FEBS Lett. 390:199-202(1996) [PubMed: 8706859] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-13, ACETYLATION AT SER-1.
[3]"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-1.

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Cross-references

Sequence databases

PIRS48157.

3D structure databases

HSSPHSSP built from PDB template 1HEU based on UniProtKB P00327.
SMRP80338. Positions 1-374.
ModBaseSearch...

Phylogenomic databases

HOVERGENP80338.

Enzyme and pathway databases

BRENDA1.1.1.1. 39275.

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_STRCA
AccessionPrimary (citable) accession number: P80338
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 54 of the entry and version 1 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