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P11766

- ADHX_HUMAN

UniProt

P11766 - ADHX_HUMAN

Protein

Alcohol dehydrogenase class-3

Gene

ADH5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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

    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

    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-succinyllysineBy similarity
    Modified residuei247 – 2471PhosphoserineBy similarity
    Modified residuei315 – 3151N6-succinyllysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti167 – 1671D → Y in AAA51597. (PubMed:2679557)Curated
    Sequence conflicti246 – 2461F → L in AAA51597. (PubMed:2679557)Curated

    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 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.

    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

    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: October 1, 2014
    This is version 168 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