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P19631 (ADH1_COTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Alcohol dehydrogenase 1
EC=1.1.1.1
Alternative name(s):
ADH3
Alcohol dehydrogenase subunit alpha
Gene names
Name:ADH1
OrganismCoturnix coturnix japonica (Japanese quail) (Coturnix japonica)
Taxonomic identifier93934 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Perdicinae › Coturnix

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

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

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionalcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

nucleotide binding

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Alcohol dehydrogenase 1
PRO_0000160673

Regions

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

Sites

Metal binding461Zinc 1; catalytic
Metal binding671Zinc 1; catalytic
Metal binding971Zinc 2
Metal binding1001Zinc 2
Metal binding1031Zinc 2
Metal binding1111Zinc 2
Metal binding1751Zinc 1; catalytic
Binding site2241NAD By similarity
Binding site2291NAD By similarity
Binding site3701NAD By similarity

Amino acid modifications

Modified residue11N-acetylserine Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19631 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 61DA4EA003DEEF7A

FASTA37539,808
        10         20         30         40         50         60 
STAGKVIKCK AAVLWEANKP FSLEEVEVAP PKAHEVRIKI VATGICRSDD HVVTGALAMP 

        70         80         90        100        110        120 
FPVILGHEAA GVVESVGEKV TLLKPGDAVI PLFVPQCGEC RSCLSTKGNL CIKNDLSSSP 

       130        140        150        160        170        180 
TGLMADGTTR FTCKGKAIHH FIGTSTFTEY TVVHETAAAK IDSAAPLEKV CLIGCGFSTG 

       190        200        210        220        230        240 
YGAVLQTAKV EPGSTCAVFG LGGVGLSVVM GCKAAGASRI IAIDINKDKF AKAKELGATE 

       250        260        270        280        290        300 
CVNPKDFKKP IHEVLTEMTG KGVDYSFEVI GRIETMTEAL ASCHYNYGVS VIVGVPPAAQ 

       310        320        330        340        350        360 
KISFDPMLIF SGRTWKGSVF GGWKSKDAVP KLVADYMKKK FVLDPLITHT LPFTKINEGF 

       370 
DLLRTGKSIR TVLVL

« Hide

References

[1]"Avian alcohol dehydrogenase. Characterization of the quail enzyme, functional interpretations, and relationships to the different classes of mammalian alcohol dehydrogenase."
Kaiser R., Nussrallah B., Dam R., Wagner F.W., Joernvall H.
Biochemistry 29:8365-8371(1990) [PubMed: 2252897] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA35837.

3D structure databases

ProteinModelPortalP19631.
SMRP19631. Positions 1-375.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000195.

Family and domain databases

InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11695. ADH_Sf_Zn. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. GroES_like. 2 hits.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH1_COTJA
AccessionPrimary (citable) accession number: P19631
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: December 14, 2011
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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