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Protein

Alcohol dehydrogenase class-3

Gene

ADH5

Organism
Homo sapiens (Human)
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+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi45Zinc 1; catalytic1 Publication1
Metal bindingi67Zinc 1; catalytic1 Publication1
Metal bindingi97Zinc 21 Publication1
Metal bindingi100Zinc 21 Publication1
Metal bindingi103Zinc 21 Publication1
Metal bindingi111Zinc 21 Publication1
Sitei115Important for FDH activity and activation by fatty acids1
Metal bindingi174Zinc 1; catalytic1

GO - Molecular functioni

  • alcohol dehydrogenase (NAD) activity Source: UniProtKB-EC
  • electron carrier activity Source: UniProtKB
  • fatty acid binding Source: UniProtKB
  • formaldehyde dehydrogenase activity Source: UniProtKB
  • S-(hydroxymethyl)glutathione dehydrogenase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

BioCyciZFISH:HS10601-MONOMER.
ReactomeiR-HSA-71384. Ethanol oxidation.
SABIO-RKP11766.

Chemistry databases

SwissLipidsiSLP:000000500.

Names & Taxonomyi

Protein namesi
Recommended name:
Alcohol dehydrogenase class-3 (EC:1.1.1.1)
Alternative name(s):
Alcohol dehydrogenase 5
Alcohol dehydrogenase class chi chain
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:ADH5Imported
Synonyms:ADHX, FDH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:253. ADH5.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi115R → A or D: Loss of FDH activity and loss of activation by fatty acids. 2 Publications1

Organism-specific databases

DisGeNETi128.
OpenTargetsiENSG00000197894.
PharmGKBiPA24574.

Chemistry databases

ChEMBLiCHEMBL4116.
DrugBankiDB00898. Ethanol.

Polymorphism and mutation databases

DMDMi113408.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001607592 – 374Alcohol dehydrogenase class-3Add BLAST373

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei233N6-succinyllysineBy similarity1
Modified residuei247PhosphoserineCombined sources1
Modified residuei315N6-succinyllysineBy similarity1
Modified residuei324PhosphoserineCombined sources1
Modified residuei351PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP11766.
PaxDbiP11766.
PeptideAtlasiP11766.
PRIDEiP11766.

2D gel databases

REPRODUCTION-2DPAGEIPI00746777.

PTM databases

iPTMnetiP11766.
PhosphoSitePlusiP11766.
SwissPalmiP11766.

Expressioni

Gene expression databases

BgeeiENSG00000197894.
CleanExiHS_ADH5.
ExpressionAtlasiP11766. baseline and differential.
GenevisibleiP11766. HS.

Organism-specific databases

HPAiHPA044578.
HPA061919.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi106640. 18 interactors.
IntActiP11766. 8 interactors.
MINTiMINT-1374117.
STRINGi9606.ENSP00000296412.

Chemistry databases

BindingDBiP11766.

Structurei

Secondary structure

1374
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 13Combined sources8
Beta strandi21 – 27Combined sources7
Beta strandi34 – 43Combined sources10
Helixi46 – 52Combined sources7
Beta strandi61 – 63Combined sources3
Beta strandi68 – 76Combined sources9
Beta strandi88 – 91Combined sources4
Beta strandi98 – 100Combined sources3
Helixi101 – 104Combined sources4
Helixi115 – 119Combined sources5
Beta strandi129 – 132Combined sources4
Beta strandi135 – 138Combined sources4
Turni141 – 143Combined sources3
Beta strandi146 – 153Combined sources8
Helixi154 – 156Combined sources3
Beta strandi157 – 159Combined sources3
Helixi166 – 169Combined sources4
Helixi170 – 173Combined sources4
Helixi175 – 184Combined sources10
Turni185 – 187Combined sources3
Beta strandi194 – 198Combined sources5
Helixi202 – 214Combined sources13
Beta strandi217 – 222Combined sources6
Helixi226 – 228Combined sources3
Helixi229 – 235Combined sources7
Beta strandi238 – 241Combined sources4
Helixi243 – 245Combined sources3
Helixi250 – 257Combined sources8
Beta strandi262 – 267Combined sources6
Helixi272 – 280Combined sources9
Turni284 – 286Combined sources3
Beta strandi288 – 291Combined sources4
Beta strandi301 – 303Combined sources3
Helixi306 – 309Combined sources4
Beta strandi313 – 316Combined sources4
Helixi319 – 321Combined sources3
Helixi324 – 336Combined sources13
Helixi343 – 345Combined sources3
Beta strandi346 – 351Combined sources6
Helixi352 – 354Combined sources3
Helixi355 – 363Combined sources9
Beta strandi368 – 373Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M6HX-ray2.00A/B2-374[»]
1M6WX-ray2.30A/B2-374[»]
1MA0X-ray2.30A/B2-374[»]
1MC5X-ray2.60A/B1-374[»]
1MP0X-ray2.20A/B2-374[»]
1TEHX-ray2.70A/B2-374[»]
2FZEX-ray1.90A/B2-374[»]
2FZWX-ray1.84A/B2-374[»]
3QJ5X-ray1.90A/B2-374[»]
ProteinModelPortaliP11766.
SMRiP11766.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11766.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
GeneTreeiENSGT00430000030800.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP11766.
KOiK00121.
OMAiNPGREAM.
OrthoDBiEOG091G08N3.
PhylomeDBiP11766.
TreeFamiTF300429.

Family and domain databases

CDDicd08300. alcohol_DH_class_III. 1 hit.
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.

P11766-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANEVIKCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKII ATAVCHTDAY
60 70 80 90 100
TLSGADPEGC FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC
110 120 130 140 150
KFCLNPKTNL CQKIRVTQGK GLMPDGTSRF TCKGKTILHY MGTSTFSEYT
160 170 180 190 200
VVADISVAKI DPLAPLDKVC LLGCGISTGY GAAVNTAKLE PGSVCAVFGL
210 220 230 240 250
GGVGLAVIMG CKVAGASRII GVDINKDKFA RAKEFGATEC INPQDFSKPI
260 270 280 290 300
QEVLIEMTDG GVDYSFECIG NVKVMRAALE ACHKGWGVSV VVGVAASGEE
310 320 330 340 350
IATRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTHNL
360 370
SFDEINKAFE LMHSGKSIRT VVKI
Length:374
Mass (Da):39,724
Last modified:January 23, 2007 - v4
Checksum:iF4F823B4A609C952
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti167D → Y in AAA51597 (PubMed:2679557).Curated1
Sequence conflicti246F → L in AAA51597 (PubMed:2679557).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025823163L → S.1 PublicationCorresponds to variant rs28730623dbSNPEnsembl.1
Natural variantiVAR_025824309V → I.1 PublicationCorresponds to variant rs28730628dbSNPEnsembl.1
Natural variantiVAR_048199353D → E.Corresponds to variant rs16996593dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30471 mRNA. Translation: AAA79018.1.
M29872 mRNA. Translation: AAA51597.1.
M81118
, M81112, M81113, M81114, M81115, M81116, M81117 Genomic DNA. Translation: AAA51596.1.
CR541689 mRNA. Translation: CAG46490.1.
BT019832 mRNA. Translation: AAV38635.1.
AY987960 Genomic DNA. Translation: AAX81412.1.
BC014665 mRNA. Translation: AAH14665.1.
CCDSiCCDS47111.1.
PIRiJH0789. DEHUC2.
RefSeqiNP_000662.3. NM_000671.4.
UniGeneiHs.78989.

Genome annotation databases

EnsembliENST00000296412; ENSP00000296412; ENSG00000197894.
GeneIDi128.
KEGGihsa:128.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30471 mRNA. Translation: AAA79018.1.
M29872 mRNA. Translation: AAA51597.1.
M81118
, M81112, M81113, M81114, M81115, M81116, M81117 Genomic DNA. Translation: AAA51596.1.
CR541689 mRNA. Translation: CAG46490.1.
BT019832 mRNA. Translation: AAV38635.1.
AY987960 Genomic DNA. Translation: AAX81412.1.
BC014665 mRNA. Translation: AAH14665.1.
CCDSiCCDS47111.1.
PIRiJH0789. DEHUC2.
RefSeqiNP_000662.3. NM_000671.4.
UniGeneiHs.78989.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M6HX-ray2.00A/B2-374[»]
1M6WX-ray2.30A/B2-374[»]
1MA0X-ray2.30A/B2-374[»]
1MC5X-ray2.60A/B1-374[»]
1MP0X-ray2.20A/B2-374[»]
1TEHX-ray2.70A/B2-374[»]
2FZEX-ray1.90A/B2-374[»]
2FZWX-ray1.84A/B2-374[»]
3QJ5X-ray1.90A/B2-374[»]
ProteinModelPortaliP11766.
SMRiP11766.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106640. 18 interactors.
IntActiP11766. 8 interactors.
MINTiMINT-1374117.
STRINGi9606.ENSP00000296412.

Chemistry databases

BindingDBiP11766.
ChEMBLiCHEMBL4116.
DrugBankiDB00898. Ethanol.
SwissLipidsiSLP:000000500.

PTM databases

iPTMnetiP11766.
PhosphoSitePlusiP11766.
SwissPalmiP11766.

Polymorphism and mutation databases

DMDMi113408.

2D gel databases

REPRODUCTION-2DPAGEIPI00746777.

Proteomic databases

EPDiP11766.
PaxDbiP11766.
PeptideAtlasiP11766.
PRIDEiP11766.

Protocols and materials databases

DNASUi128.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296412; ENSP00000296412; ENSG00000197894.
GeneIDi128.
KEGGihsa:128.

Organism-specific databases

CTDi128.
DisGeNETi128.
GeneCardsiADH5.
HGNCiHGNC:253. ADH5.
HPAiHPA044578.
HPA061919.
MIMi103710. gene.
neXtProtiNX_P11766.
OpenTargetsiENSG00000197894.
PharmGKBiPA24574.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0022. Eukaryota.
COG1062. LUCA.
GeneTreeiENSGT00430000030800.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP11766.
KOiK00121.
OMAiNPGREAM.
OrthoDBiEOG091G08N3.
PhylomeDBiP11766.
TreeFamiTF300429.

Enzyme and pathway databases

BioCyciZFISH:HS10601-MONOMER.
ReactomeiR-HSA-71384. Ethanol oxidation.
SABIO-RKP11766.

Miscellaneous databases

ChiTaRSiADH5. human.
EvolutionaryTraceiP11766.
GeneWikiiADH5.
GenomeRNAii128.
PROiP11766.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197894.
CleanExiHS_ADH5.
ExpressionAtlasiP11766. baseline and differential.
GenevisibleiP11766. HS.

Family and domain databases

CDDicd08300. alcohol_DH_class_III. 1 hit.
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...

Entry informationi

Entry nameiADHX_HUMAN
AccessioniPrimary (citable) accession number: P11766
Secondary accession number(s): Q6FHR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 189 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

There are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.