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P19854 (ADHX_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 85. 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 class-3
EC=1.1.1.1
Alternative name(s):
Alcohol dehydrogenase 5
Alcohol dehydrogenase class-III
Glutathione-dependent formaldehyde dehydrogenase
Short name=FALDH
Short name=FDH
Short name=GSH-FDH
EC=1.1.1.-
S-(hydroxymethyl)glutathione dehydrogenase
EC=1.1.1.284
Gene names
Name:ADH5
OrganismEquus caballus (Horse) [Complete proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Perissodactyla › Equidae › Equus

Protein attributes

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

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.

Subcellular location

Cytoplasm.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1 Ref.2
Chain2 – 374373Alcohol dehydrogenase class-3
PRO_0000160758

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-acetylserine Ref.1 Ref.2
Modified residue3661N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P19854 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 190D38896ED9D094

FASTA37439,572
        10         20         30         40         50         60 
MSAEVIKCKA AVAWEAGKPV SIEEVEVAPP KAHEVRIKII ATAVCHTDAY TLSGADPEGS 

        70         80         90        100        110        120 
FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPQTNL CQKIRTTQGK 

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

       190        200        210        220        230        240 
GAAVNTAKVE PGSTCAIFGL GGVGLAVIMG CKVAGASRII GVDINKDKFA KAKEFGASEC 

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

       310        320        330        340        350        360 
IATRPFQLVT GRTWKGTAFG GWKSVESIPK LVSEYMSKKI KVDEFVTHSL SFDQINEAFE 

       370 
LMHAGKSIRT VVKL

« Hide

References

[1]"Characteristics of mammalian class III alcohol dehydrogenases, an enzyme less variable than the traditional liver enzyme of class I."
Kaiser R., Holmquist B., Vallee B.L., Joernvall H.
Biochemistry 28:8432-8438(1989) [PubMed: 2690942] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-374, ACETYLATION AT SER-2.
[2]"Acetylated N-terminal structures of class III alcohol dehydrogenases. Differences among the three enzyme classes."
Fairwell T., Julia P., Kaiser R., Holmquist B., Pares X., Vallee B.L., Joernvall H.
FEBS Lett. 222:99-103(1987) [PubMed: 3653405] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-7, ACETYLATION AT SER-2.
+Additional computationally mapped references.

Cross-references

Sequence databases

PIRA33419.
S02617.

3D structure databases

ProteinModelPortalP19854.
SMRP19854. Positions 4-374.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000195.

Family and domain databases

InterProIPR014183. ADH_3.
IPR013149. 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.
TIGRFAMsTIGR02818. Adh_III_F_hyde. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADHX_HORSE
AccessionPrimary (citable) accession number: P19854
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: April 3, 2007
Last modified: December 14, 2011
This is version 85 of the entry and version 2 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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