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Reviewed, UniProtKB/Swiss-Prot O19053 (ADHX_RABIT)

Last modified October 13, 2009. Version 62. 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 class-3
    EC=1.1.1.1
Alternative name(s):
    Alcohol dehydrogenase class-III
    Alcohol dehydrogenase 5
    S-(hydroxymethyl)glutathione dehydrogenase
    EC=1.1.1.284
    Glutathione-dependent formaldehyde dehydrogenase
      Short name=GSH-FDH
      Short name=FALDH
      Short name=FDH
    EC=1.1.1.-
Gene names
Name: ADH5
Synonyms: ADH3
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

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Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.

Catalytic activity

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

S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.

Cofactor

Binds 2 zinc ions per subunit.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Sequence similarities

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 374373Alcohol dehydrogenase class-3
PRO_0000160761

Sites

Metal binding451Zinc 1; catalytic
Metal binding671Zinc 1; catalytic
Metal binding971Zinc 2
Metal binding1001Zinc 2
Metal binding1031Zinc 2
Metal binding1111Zinc 2
Metal binding1741Zinc 1; catalytic
Site1151Important for FDH activity and activation by fatty acids By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3661N6-acetyllysine By similarity

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Sequences

Sequence LengthMass (Da)Tools
O19053-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CC89BDC4CDD4FB83

FASTA37439,596
        10         20         30         40         50         60 
MANKVIKCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKIF ATAVCHTDAY TLSGADPEGC 

        70         80         90        100        110        120 
FPVILGHEGA GIVESVGEGV TNLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK 

       130        140        150        160        170        180 
GLMPDGTSRF TCKGKTILHY MGTSTFSEYT VVADISVAKI DPSAPLDKVC LLGCGISTGY 

       190        200        210        220        230        240 
GAALNTAKVE PGSTCAVFGL GGVGLAAIMG CKAAGASRII AVDINKDKFA RAKEFGATEC 

       250        260        270        280        290        300 
INPQDFSKPI QEVLVEKTDG GVDYSFECIG NVKVMRAALE ACHKGWGVSV VVGVAGAGEE 

       310        320        330        340        350        360 
ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI NVDEFVTNTL SFDQINEAFE 

       370 
LMHSGKSIRT VVKI

« Hide

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References

[1]"Structural and functional divergence of class II alcohol dehydrogenase -- cloning and characterisation of rabbit liver isoforms of the enzyme."
Svensson S., Hedberg J., Hoeoeg J.-O.
Eur. J. Biochem. 251:236-243(1998) [PubMed: 9492289] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: New Zealand white.
Tissue: Liver.

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Cross-references

Sequence databases

Y15406 mRNA. Translation: CAA75606.1.
RefSeqNP_001076093.1.
UniGeneOcu.3296

3D structure databases

HSSPHSSP built from PDB template 1M6H based on UniProtKB P11766.
SMRO19053. Positions 2-374.
ModBaseSearch...

Genome annotation databases

GeneID100009307.

Organism-specific databases

CTD100009307.

Phylogenomic databases

HOVERGENO19053.

Enzyme and pathway databases

BRENDA1.1.1.1. 255.
1.1.1.284. 255.

Family and domain databases

InterProIPR014183. ADH_3.
IPR013154. 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]
TIGRFAMsTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameADHX_RABIT
AccessionPrimary (citable) accession number: O19053
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 13, 2009
This is version 62 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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