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Reviewed, UniProtKB/Swiss-Prot P85440 (ADH1_CATRO)

Last modified November 4, 2008. Version 6. 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

Names and origin

Protein namesRecommended name:
    Alcohol dehydrogenase 1
    EC=1.1.1.1
OrganismCatharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Taxonomic identifier4058 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsGentianalesApocynaceaeRauvolfioideaeVinceaeCatharanthus

Protein attributes

Sequence length31 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is not processed.
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 By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

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

Ontologies

Keywords

   Cellular componentCytoplasm
   LigandMetal-binding
NAD
Zinc
   Molecular functionOxidoreductase
   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-KW

   Molecular functionalcohol dehydrogenase 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

Chain‹1 – ›31›31Alcohol dehydrogenase 1
PRO_0000324677

Sites

Metal binding71Zinc 2 By similarity

Experimental info

Non-adjacent residues11 – 122
Non-terminal residue11
Non-terminal residue311

Sequences

Sequence LengthMass (Da)Tools
P85440-1 [UniParc].

Last modified March 18, 2008. Version 1.
Checksum: 5EF8D543503B569D

FASTA313,470
        10         20         30 
SEESNLCDLL RDYDKPAQEV IAEMTDGGVD R 

« Hide

References

[1]Varman P.A.M., Ranjitha Kumari B.D.
Submitted (JAN-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE.

Cross-references

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR002328. AlcDHase_Zn_CS.
[Graphical view]
PROSITEPS00059. ADH_ZINC. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADH1_CATRO
AccessionPrimary (citable) accession number: P85440
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: November 4, 2008
This is version 6 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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