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Protein

Alcohol dehydrogenase class-3

Gene

Adh5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Zinc 1; catalyticBy similarity
Metal bindingi67 – 671Zinc 1; catalyticBy similarity
Metal bindingi97 – 971Zinc 2By similarity
Metal bindingi100 – 1001Zinc 2By similarity
Metal bindingi103 – 1031Zinc 2By similarity
Metal bindingi111 – 1111Zinc 2By similarity
Sitei115 – 1151Important for FDH activity and activation by fatty acidsBy similarity
Metal bindingi174 – 1741Zinc 1; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • ethanol catabolic process Source: RGD
  • ethanol oxidation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-71384. Ethanol oxidation.
SABIO-RKP12711.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class-3 (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase 2
Alcohol dehydrogenase 5
Alcohol dehydrogenase B2
Short name:
ADH-B2
Alcohol dehydrogenase class-III
Glutathione-dependent formaldehyde dehydrogenase (EC:1.1.1.-)
Short name:
FALDH
Short name:
FDH
Short name:
GSH-FDH
S-(hydroxymethyl)glutathione dehydrogenase (EC:1.1.1.284)
Gene namesi
Name:Adh5
Synonyms:Adh-2, Adh2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi2292706. Adh5.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 374373Alcohol dehydrogenase class-3PRO_0000160762Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei233 – 2331N6-succinyllysineBy similarity
Modified residuei247 – 2471PhosphoserineBy similarity
Modified residuei315 – 3151N6-succinyllysineBy similarity
Modified residuei324 – 3241PhosphoserineBy similarity
Modified residuei351 – 3511PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP12711.
PRIDEiP12711.

PTM databases

iPTMnetiP12711.

Expressioni

Gene expression databases

ExpressionAtlasiP12711. baseline and differential.
GenevisibleiP12711. RN.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017252.

Structurei

3D structure databases

ProteinModelPortaliP12711.
SMRiP12711. Positions 2-374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
GeneTreeiENSGT00430000030800.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP12711.
KOiK00121.
OMAiMITHVLK.
OrthoDBiEOG72NRQ6.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12711-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANQVIRCKA AVAWEAGKPL SIEEIEVAPP QAHEVRIKII ATAVCHTDAY
60 70 80 90 100
TLSGADPEGC FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC
110 120 130 140 150
KFCLNPKTNL CQKIRVTQGK GLMPDGTSRF TCKGKPILHF MGTSTFSEYT
160 170 180 190 200
VVADISVAKI DPSAPLDKVC LLGCGISTGY GAAVNTAKVE PGSTCAVFGL
210 220 230 240 250
GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGATEC INPQDFSKSI
260 270 280 290 300
QEVLIEMTDG GVDFSFECIG NVKVMRSALE AAHKGWGVSV VVGVAASGEE
310 320 330 340 350
ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTGNL
360 370
SFDQINKAFD LMHSGNSIRT VLKM
Length:374
Mass (Da):39,576
Last modified:March 20, 2007 - v2
Checksum:iD97A768DEED84C96
GO

Sequence cautioni

The sequence AAH83724.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti374 – 3741M → L AA sequence (PubMed:3278908).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083724 mRNA. Translation: AAH83724.1. Different initiation.
PIRiS00331. DERTA.
RefSeqiNP_001119592.1. NM_001126120.1.
UniGeneiRn.222115.

Genome annotation databases

EnsembliENSRNOT00000017252; ENSRNOP00000017252; ENSRNOG00000046357.
GeneIDi100145871.
KEGGirno:100145871.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083724 mRNA. Translation: AAH83724.1. Different initiation.
PIRiS00331. DERTA.
RefSeqiNP_001119592.1. NM_001126120.1.
UniGeneiRn.222115.

3D structure databases

ProteinModelPortaliP12711.
SMRiP12711. Positions 2-374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017252.

PTM databases

iPTMnetiP12711.

Proteomic databases

PaxDbiP12711.
PRIDEiP12711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017252; ENSRNOP00000017252; ENSRNOG00000046357.
GeneIDi100145871.
KEGGirno:100145871.

Organism-specific databases

CTDi128.
RGDi2292706. Adh5.

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
GeneTreeiENSGT00430000030800.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP12711.
KOiK00121.
OMAiMITHVLK.
OrthoDBiEOG72NRQ6.

Enzyme and pathway databases

ReactomeiR-RNO-71384. Ethanol oxidation.
SABIO-RKP12711.

Miscellaneous databases

PROiP12711.

Gene expression databases

ExpressionAtlasiP12711. baseline and differential.
GenevisibleiP12711. RN.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. ADH_3.
IPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 2 hits.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.

Entry informationi

Entry nameiADHX_RAT
AccessioniPrimary (citable) accession number: P12711
Secondary accession number(s): Q5XIF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: March 20, 2007
Last modified: July 6, 2016
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.