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P11766

- ADHX_HUMAN

UniProt

P11766 - ADHX_HUMAN

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Protein

Alcohol dehydrogenase class-3

Gene
ADH5, ADHX, FDH
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 2 zinc ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Zinc 1; catalytic1 Publication
Metal bindingi67 – 671Zinc 1; catalytic1 Publication
Metal bindingi97 – 971Zinc 21 Publication
Metal bindingi100 – 1001Zinc 21 Publication
Metal bindingi103 – 1031Zinc 21 Publication
Metal bindingi111 – 1111Zinc 21 Publication
Sitei115 – 1151Important for FDH activity and activation by fatty acids
Metal bindingi174 – 1741Zinc 1; catalytic

GO - Molecular functioni

  1. alcohol dehydrogenase (NAD) activity Source: UniProtKB-EC
  2. electron carrier activity Source: UniProtKB
  3. fatty acid binding Source: UniProtKB
  4. formaldehyde dehydrogenase activity Source: UniProtKB
  5. S-(hydroxymethyl)glutathione dehydrogenase activity Source: UniProtKB
  6. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. ethanol catabolic process Source: Ensembl
  3. ethanol oxidation Source: InterPro
  4. formaldehyde catabolic process Source: Ensembl
  5. peptidyl-cysteine S-nitrosylation Source: Ensembl
  6. positive regulation of blood pressure Source: Ensembl
  7. respiratory system process Source: Ensembl
  8. response to lipopolysaccharide Source: Ensembl
  9. response to nitrosative stress Source: Ensembl
  10. response to redox state Source: UniProtKB
  11. retinoid metabolic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, NAD, Zinc

Enzyme and pathway databases

SABIO-RKP11766.

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:ADH5
Synonyms:ADHX, FDH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:253. ADH5.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrion Source: Ensembl
  3. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi115 – 1151R → A or D: Loss of FDH activity and loss of activation by fatty acids. 2 Publications

Organism-specific databases

PharmGKBiPA24574.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 374373Alcohol dehydrogenase class-3PRO_0000160759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei233 – 2331N6-succinyllysine By similarity
Modified residuei247 – 2471Phosphoserine By similarity
Modified residuei315 – 3151N6-succinyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP11766.
PaxDbiP11766.
PRIDEiP11766.

2D gel databases

REPRODUCTION-2DPAGEIPI00746777.

PTM databases

PhosphoSiteiP11766.

Expressioni

Gene expression databases

ArrayExpressiP11766.
BgeeiP11766.
CleanExiHS_ADH5.
GenevestigatoriP11766.

Organism-specific databases

HPAiHPA044578.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi106640. 15 interactions.
IntActiP11766. 8 interactions.
MINTiMINT-1374117.
STRINGi9606.ENSP00000296412.

Structurei

Secondary structure

1
374
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138
Beta strandi21 – 277
Beta strandi34 – 4310
Helixi46 – 527
Beta strandi61 – 633
Beta strandi68 – 769
Beta strandi88 – 914
Beta strandi98 – 1003
Helixi101 – 1044
Helixi115 – 1195
Beta strandi129 – 1324
Beta strandi135 – 1384
Turni141 – 1433
Beta strandi146 – 1538
Helixi154 – 1563
Beta strandi157 – 1593
Helixi166 – 1694
Helixi170 – 1734
Helixi175 – 18410
Turni185 – 1873
Beta strandi194 – 1985
Helixi202 – 21413
Beta strandi217 – 2226
Helixi226 – 2283
Helixi229 – 2357
Beta strandi238 – 2414
Helixi243 – 2453
Helixi250 – 2578
Beta strandi262 – 2676
Helixi272 – 2809
Turni284 – 2863
Beta strandi288 – 2914
Beta strandi301 – 3033
Helixi306 – 3094
Beta strandi313 – 3164
Helixi319 – 3213
Helixi324 – 33613
Helixi343 – 3453
Beta strandi346 – 3516
Helixi352 – 3543
Helixi355 – 3639
Beta strandi368 – 3736

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 2-374.

Miscellaneous databases

EvolutionaryTraceiP11766.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1062.
HOGENOMiHOG000294674.
HOVERGENiHBG000195.
InParanoidiP11766.
KOiK00121.
OMAiAWKSGAP.
OrthoDBiEOG72NRQ6.
PhylomeDBiP11766.
TreeFamiTF300429.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR014183. 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]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 2 hits.
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

MANEVIKCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKII ATAVCHTDAY    50
TLSGADPEGC FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC 100
KFCLNPKTNL CQKIRVTQGK GLMPDGTSRF TCKGKTILHY MGTSTFSEYT 150
VVADISVAKI DPLAPLDKVC LLGCGISTGY GAAVNTAKLE PGSVCAVFGL 200
GGVGLAVIMG CKVAGASRII GVDINKDKFA RAKEFGATEC INPQDFSKPI 250
QEVLIEMTDG GVDYSFECIG NVKVMRAALE ACHKGWGVSV VVGVAASGEE 300
IATRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTHNL 350
SFDEINKAFE LMHSGKSIRT VVKI 374
Length:374
Mass (Da):39,724
Last modified:January 23, 2007 - v4
Checksum:iF4F823B4A609C952
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti163 – 1631L → S.1 Publication
Corresponds to variant rs28730623 [ dbSNP | Ensembl ].
VAR_025823
Natural varianti309 – 3091V → I.1 Publication
Corresponds to variant rs28730628 [ dbSNP | Ensembl ].
VAR_025824
Natural varianti353 – 3531D → E.
Corresponds to variant rs16996593 [ dbSNP | Ensembl ].
VAR_048199

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671D → Y in AAA51597. 1 Publication
Sequence conflicti246 – 2461F → L in AAA51597. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc003hui.3. human.

Polymorphism databases

DMDMi113408.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS47111.1.
PIRi JH0789. DEHUC2.
RefSeqi NP_000662.3. NM_000671.4.
UniGenei Hs.78989.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1M6H X-ray 2.00 A/B 2-374 [» ]
1M6W X-ray 2.30 A/B 2-374 [» ]
1MA0 X-ray 2.30 A/B 2-374 [» ]
1MC5 X-ray 2.60 A/B 1-374 [» ]
1MP0 X-ray 2.20 A/B 2-374 [» ]
1TEH X-ray 2.70 A/B 2-374 [» ]
2FZE X-ray 1.90 A/B 2-374 [» ]
2FZW X-ray 1.84 A/B 2-374 [» ]
3QJ5 X-ray 1.90 A/B 2-374 [» ]
ProteinModelPortali P11766.
SMRi P11766. Positions 2-374.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106640. 15 interactions.
IntActi P11766. 8 interactions.
MINTi MINT-1374117.
STRINGi 9606.ENSP00000296412.

Chemistry

BindingDBi P11766.
ChEMBLi CHEMBL2096668.
DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei P11766.

Polymorphism databases

DMDMi 113408.

2D gel databases

REPRODUCTION-2DPAGE IPI00746777.

Proteomic databases

MaxQBi P11766.
PaxDbi P11766.
PRIDEi P11766.

Protocols and materials databases

DNASUi 128.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296412 ; ENSP00000296412 ; ENSG00000197894 .
GeneIDi 128.
KEGGi hsa:128.
UCSCi uc003hui.3. human.

Organism-specific databases

CTDi 128.
GeneCardsi GC04M099992.
HGNCi HGNC:253. ADH5.
HPAi HPA044578.
MIMi 103710. gene.
neXtProti NX_P11766.
PharmGKBi PA24574.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1062.
HOGENOMi HOG000294674.
HOVERGENi HBG000195.
InParanoidi P11766.
KOi K00121.
OMAi AWKSGAP.
OrthoDBi EOG72NRQ6.
PhylomeDBi P11766.
TreeFami TF300429.

Enzyme and pathway databases

SABIO-RK P11766.

Miscellaneous databases

ChiTaRSi ADH5. human.
EvolutionaryTracei P11766.
GeneWikii ADH5.
GenomeRNAii 128.
NextBioi 511.
PROi P11766.
SOURCEi Search...

Gene expression databases

ArrayExpressi P11766.
Bgeei P11766.
CleanExi HS_ADH5.
Genevestigatori P11766.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProi IPR014183. 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 ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
Pfami PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 2 hits.
TIGRFAMsi TIGR02818. adh_III_F_hyde. 1 hit.
PROSITEi PS00059. ADH_ZINC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning and comparative mapping of a human class III (chi) alcohol dehydrogenase cDNA."
    Giri P.R., Krug J.F., Kozak C., Moretti T., O'Brien S.J., Seuanez H.N., Goldman D.
    Biochem. Biophys. Res. Commun. 164:453-460(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning and characterization of the ADH5 gene encoding human alcohol dehydrogenase 5, formaldehyde dehydrogenase."
    Hur M.W., Edenberg H.J.
    Gene 121:305-311(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. NIEHS SNPs program
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-163 AND ILE-309.
  7. "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: B-cell.
  8. "Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes."
    Kaiser R., Holmquist B., Hempel J., Vallee B.L., Joernvall H.
    Biochemistry 27:1132-1140(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-374.
    Tissue: Liver.
  9. "Role of arginine 115 in fatty acid activation and formaldehyde dehydrogenase activity of human class III alcohol dehydrogenase."
    Holmquist B., Moulis J.-M., Engeland K., Vallee B.L.
    Biochemistry 32:5139-5144(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF ARG-115.
  10. "Mutation of Arg-115 of human class III alcohol dehydrogenase: a binding site required for formaldehyde dehydrogenase activity and fatty acid activation."
    Engeland K., Hoeoeg J.-O., Holmquist B., Estonius M., Joernvall H., Vallee B.L.
    Proc. Natl. Acad. Sci. U.S.A. 90:2491-2494(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-115.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase."
    Yang Z.-N., Bosron W.F., Hurley T.D.
    J. Mol. Biol. 265:330-343(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).

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: July 9, 2014
This is version 167 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

External Data

Dasty 3

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