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Reviewed, UniProtKB/Swiss-Prot P12711 (ADHX_RAT)

Last modified February 9, 2010. Version 85. 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
    Alcohol dehydrogenase 2
    Alcohol dehydrogenase B2
      Short name=ADH-B2
    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: Adh-2, Adh2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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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 protein 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 By similarity.

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

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

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Ontologies

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

Inferred from electronic annotation. Source: InterPro

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionS-(hydroxymethyl)glutathione dehydrogenase activity

Inferred from electronic annotation. Source: EC

alcohol dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.3
Chain2 – 374373Alcohol dehydrogenase class-3
PRO_0000160762

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 Ref.2 Ref.3

Experimental info

Sequence conflict3741M → L AA sequence Ref.2

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Sequences

Sequence LengthMass (Da)Tools
P12711-1 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: D97A768DEED84C96

FASTA37439,576
        10         20         30         40         50         60 
MANQVIRCKA AVAWEAGKPL SIEEIEVAPP QAHEVRIKII ATAVCHTDAY TLSGADPEGC 

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

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

       190        200        210        220        230        240 
GAAVNTAKVE PGSTCAVFGL GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGATEC 

       250        260        270        280        290        300 
INPQDFSKSI QEVLIEMTDG GVDFSFECIG NVKVMRSALE AAHKGWGVSV VVGVAASGEE 

       310        320        330        340        350        360 
ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTGNL SFDQINKAFD 

       370 
LMHSGNSIRT VLKM

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References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Heart.
[2]"Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases."
Julia P., Pares X., Joernvall H.
Eur. J. Biochem. 172:73-83(1988) [PubMed: 3278908] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-374.
Tissue: Liver.
[3]"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 ALA-2.
[4]"Model for the structure of formaldehyde dehydrogenase based on alcohol dehydrogenase."
Lapatto R.
Int. J. Biol. Macromol. 13:73-76(1991) [PubMed: 1888714] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC083724 mRNA. Translation: AAH83724.1. Different initiation.
IPIIPI00568787.
PIRDERTA. S00331.
RefSeqNP_001119592.1.
UniGeneRn.222115

3D structure databases

SMRP12711. Positions 2-374.
ModBaseSearch...

Protein-protein interaction databases

STRINGP12711.

Proteomic databases

PRIDEP12711.

Genome annotation databases

EnsemblENSRNOT00000017252; ENSRNOP00000017252; ENSRNOG00000033854; Rattus norvegicus. [Genome view]
GeneID100145871.
KEGGrno:100145871.
NMPDRfig|10116.3.peg.17090.

Organism-specific databases

CTD100145871.
RGD2292706. Adh5.

Phylogenomic databases

HOVERGENP12711.
PhylomeDBP12711.

Enzyme and pathway databases

BRENDA1.1.1.1. 248.
1.1.1.284. 248.

Gene expression databases

ArrayExpressP12711.
GenevestigatorP12711.
GermOnlineENSRNOG00000033854. Rattus norvegicus.

Family and domain databases

InterProIPR014183. ADH_3.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn.
IPR013149. ADH_Zn-bd.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[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_RAT
AccessionPrimary (citable) accession number: P12711
Secondary accession number(s): Q5XIF8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: March 20, 2007
Last modified: February 9, 2010
This is version 85 of the entry and version 2 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