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Protein

Alcohol dehydrogenase class-3

Gene
N/A
Organism
Pisum sativum (Garden pea)
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.1 Publication
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H.1 Publication

Cofactori

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

Kineticsi

kcat is 190 min(-1) with octanol as substrate (at pH 10). kcat is 110 min(-1) with 12-OH-dodecanoic acid as substrate (at pH 10). kcat is 380 min(-1) with S-hydroxymethylglutathione as substrate (at pH 8).1 Publication
  1. KM=840 µM for octanol (at pH 10)1 Publication
  2. KM=180 µM for 12-OH-dodecanoic acid (at pH 10)1 Publication
  3. KM=6.5 µM for NAD+ (at pH 10)1 Publication
  4. KM=2 µM for S-(hydroxymethyl)glutathione (at pH 8)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi46Zinc 1; catalyticBy similarity1
    Binding sitei47NADBy similarity1
    Binding sitei48SubstrateBy similarity1
    Metal bindingi68Zinc 1; catalyticBy similarity1
    Binding sitei68SubstrateBy similarity1
    Metal bindingi69Zinc 1By similarity1
    Metal bindingi98Zinc 2By similarity1
    Metal bindingi101Zinc 2By similarity1
    Metal bindingi104Zinc 2By similarity1
    Metal bindingi112Zinc 2By similarity1
    Metal bindingi176Zinc 1; catalyticBy similarity1
    Binding sitei225NADBy similarity1
    Binding sitei230NADBy similarity1
    Binding sitei371NADBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi201 – 206NADBy similarity6
    Nucleotide bindingi294 – 296NADBy similarity3
    Nucleotide bindingi319 – 321NADBy similarity3

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionOxidoreductase
    LigandMetal-binding, NAD, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase class-3 (EC:1.1.1.11 Publication)
    Alternative name(s):
    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:1.1.1.2841 Publication)
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    Subcellular locationi

    • Cytoplasm By similarity

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001607741 – 378Alcohol dehydrogenase class-3Add BLAST378

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1N-acetylalanine2 Publications1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP80572.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP80572.
    SMRiP80572.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Family and domain databases

    CDDicd08300. alcohol_DH_class_III. 1 hit.
    InterProiView protein in InterPro
    IPR014183. ADH_3.
    IPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    PfamiView protein in Pfam
    PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    SUPFAMiSSF50129. SSF50129. 2 hits.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
    PROSITEiView protein in PROSITE
    PS00059. ADH_ZINC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P80572-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    ATQGQVITCK AAVAWEPNKP LTIEDVEVAP PQANEVRIQI LFTALCHTDA
    60 70 80 90 100
    YTLGGKDPEG LFPCILGHEA AGIVESVGEG VTDVKPGDHV IPSYQAECGE
    110 120 130 140 150
    CKFCKSPKTN LCGKVRAATG VGVMMADRKS RFSVKGKPIY HFMGTSTFSQ
    160 170 180 190 200
    YTVVHDVSVA KIHPDAPLDK VCLLGCGVPT GLGAVWNTAK VEPGSIVAIF
    210 220 230 240 250
    GLGTVGLAVA EGAKSAGASR IIGIDIDSNK YDTAKNFGVT EFINPKDHEK
    260 270 280 290 300
    PIQQVIIDLT DGGVDYSFEC LGNVSVMRSA LECCHKGWGT SVIVGVAASG
    310 320 330 340 350
    QEISTRPFQL VTGRVWKGTA FGGFKSRSQV PWLVEKYLKK EIKVDEYITH
    360 370
    NLTLLEINKA FDLLHEGQCL RCVLAVHD
    Length:378
    Mass (Da):40,489
    Last modified:July 15, 1998 - v1
    Checksum:i9ED1C511219FF45B
    GO

    Sequence databases

    PIRiS66198.

    Cross-referencesi

    Sequence databases

    PIRiS66198.

    3D structure databases

    ProteinModelPortaliP80572.
    SMRiP80572.
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiP80572.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Family and domain databases

    CDDicd08300. alcohol_DH_class_III. 1 hit.
    InterProiView protein in InterPro
    IPR014183. ADH_3.
    IPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    PfamiView protein in Pfam
    PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    SUPFAMiSSF50129. SSF50129. 2 hits.
    SSF51735. SSF51735. 1 hit.
    TIGRFAMsiTIGR02818. adh_III_F_hyde. 1 hit.
    PROSITEiView protein in PROSITE
    PS00059. ADH_ZINC. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiADHX_PEA
    AccessioniPrimary (citable) accession number: P80572
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 15, 1998
    Last modified: May 10, 2017
    This is version 94 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    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.