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Reviewed, UniProtKB/Swiss-Prot Q3ZC42 (ADHX_BOVIN)

Last modified June 16, 2009. Version 32. 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
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

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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 By similarity.

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 By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

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_0000282937

Sites

Metal binding451Zinc 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
Site1151Important for FDH activity and activation by fatty acids By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q3ZC42-1 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: 307A47ECEC560C0F

FASTA37439,677
        10         20         30         40         50         60 
MANQVIKCKA AVAWEAGKPL SIEEVEVAPP KAHEVRIKII ATAVCHTDAY TLSGADPEGN 

        70         80         90        100        110        120 
YPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK 

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

       190        200        210        220        230        240 
GAALNAAKVE PGSTCAVFGL GGVGLAVIMG CKMAGAARII GVDINKDKFA RAKEFGASEC 

       250        260        270        280        290        300 
INPQDFSKPI QEVLIEMTDG GVDYSFECIG NVKVMRAALE ACHKGWGISV VVGVAASGEE 

       310        320        330        340        350        360 
IATRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTHSL PFDQINEAFD 

       370 
LMHAGKSIRT VVKL

« Hide

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References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Thymus.

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Cross-references

Sequence databases

BC102926 mRNA. Translation: AAI02927.1.
IPIIPI00692275.
RefSeqNP_001029421.1.
UniGeneBt.49339

3D structure databases

SMRQ3ZC42. Positions 2-374.
ModBaseSearch...

Genome annotation databases

EnsemblENSBTAG00000016007. Bos taurus. [Contig view]
GeneID505515.
KEGGbta:505515.

Phylogenomic databases

HOVERGENQ3ZC42.

Enzyme and pathway databases

BRENDA1.1.1.1. 251.
1.1.1.284. 251.

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_BOVIN
AccessionPrimary (citable) accession number: Q3ZC42
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: September 27, 2005
Last modified: June 16, 2009
This is version 32 of the entry and version 1 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