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Protein

Aldehyde-alcohol dehydrogenase 2

Gene

ADH2

Organism
Entamoeba histolytica
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme has two NAD+-dependent activities: ADH and ACDH. May be a critical enzyme in the fermentative pathway.2 Publications

Catalytic activityi

An alcohol + NAD+ = an aldehyde or ketone + NADH.2 Publications
Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.2 Publications

Cofactori

Zn2+By similarity, Fe2+By similarityNote: Zinc or iron.By similarity

Kineticsi

  1. KM=80 mM for ethanol1 Publication
  2. KM=0.15 mM for acetaldehyde1 Publication
  3. KM=0.015 mM for acetyl-CoA1 Publication
  4. KM=0.15 mM for NAD+ (for ADH activity)1 Publication
  5. KM=0.05 mM for NADH (for ADH activity)1 Publication
  6. KM=0.18 mM for NADH (for ACDH activity)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei252By similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi431 – 436NADSequence analysis6

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Iron, NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde-alcohol dehydrogenase 2Curated
    Including the following 2 domains:
    Alcohol dehydrogenase2 Publications (EC:1.1.1.12 Publications)
    Short name:
    ADH2 Publications
    Acetaldehyde dehydrogenase2 Publications (EC:1.2.1.102 Publications)
    Short name:
    ACDH1 Publication
    Gene namesi
    Name:ADH2
    OrganismiEntamoeba histolytica
    Taxonomic identifieri5759 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaArchamoebaeEntamoebidaeEntamoeba

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000878351 – 870Aldehyde-alcohol dehydrogenase 2Add BLAST870

    Interactioni

    Subunit structurei

    Seems to form a rod shaped homopolymer composed of at least 20 identical subunits.1 Publication

    Protein-protein interaction databases

    STRINGi5759.rna_EHI_150490-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ24803.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi54 – 59Poly-Ala6

    Sequence similaritiesi

    In the N-terminal section; belongs to the aldehyde dehydrogenase family.Curated
    In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiKOG3857. Eukaryota.
    COG1012. LUCA.
    COG1454. LUCA.

    Family and domain databases

    Gene3Di3.40.309.10. 2 hits.
    3.40.605.10. 1 hit.
    InterProiIPR001670. ADH_Fe.
    IPR018211. ADH_Fe_CS.
    IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR012079. Bifunc_Ald-ADH.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    PF00465. Fe-ADH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000111. ALDH_ADH. 1 hit.
    SUPFAMiSSF53720. SSF53720. 2 hits.
    PROSITEiPS00913. ADH_IRON_1. 1 hit.
    PS00060. ADH_IRON_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q24803-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTQQTMTVD EHINQLVRKA QVALKEYLKP EYTQEKIDYI VKKASVAALD
    60 70 80 90 100
    QHCALAAAAV EETGRGIFED KATKNIFACE HVTHEMRHAK TVGIINVDPL
    110 120 130 140 150
    YGITEIAEPV GVVCGVTPVT NPTSTAIFKS LISIKTRNPI VFSFHPSALK
    160 170 180 190 200
    CSIMAAKIVR DAAIAAGAPE NCIQWIEFGG IEASNKLMNH PGVATILATG
    210 220 230 240 250
    GNAMVKAAYS SGKPALGVGA GNVPTYIEKT CNIKQAANDV VMSKSFDNGM
    260 270 280 290 300
    ICASEQAAII DKEIYDQVVE EMKTLGAYFI NEEEKAKLEK FMFGVNAYSA
    310 320 330 340 350
    DVNNARLNPK CPGMSPQWFA EQVGIKVPED CNIICAVCKE VGPNEPLTRE
    360 370 380 390 400
    KLSPVLAILK AENTQDGIDK AEAMVEFNGR GHSAAIHSND KAVVEKYALT
    410 420 430 440 450
    MKACRILHNT PSSQGGIGSI YNYIWPSFTL GCGSYGGNSV SANVTYHNLL
    460 470 480 490 500
    NIKRLADRRN NLQWFRVPPK IFFEPHSIRY LAELKELSKI FIVSDRMMYK
    510 520 530 540 550
    LGYVDRVMDV LKRRSNEVEI EIFIDVEPDP SIQTVQKGLA VMNTFGPDNI
    560 570 580 590 600
    IAIGGGSAMD AAKIMWLLYE HPEADFFAMK QKFIDLRKRA FKFPTMGKKA
    610 620 630 640 650
    RLICIPTTSG TGSEVTPFAV ISDHETGKKY PLADYSLTPS VAIVDPMFTM
    660 670 680 690 700
    SLPKRAIADT GLDVLVHATE AYVSVMANEY TDGLAREAVK LVFENLLKSY
    710 720 730 740 750
    NGDLEAREKM HNAATIAGMA FASAFLGMDH SMAHKVGAAF HLPHGRCVAV
    760 770 780 790 800
    LLPHVIRYNG QKPRKLAMWP KYNFYKADQR YMELAQMVGL KCNTPAEGVE
    810 820 830 840 850
    AFAKACEELM KATETITGFK KANIDEAAWM SKVPEMALLA FEDQCSPANP
    860 870
    RVPMVKDMEK ILKAAYYPIA
    Length:870
    Mass (Da):95,659
    Last modified:November 1, 1997 - v1
    Checksum:i66733AD08CE3D0A5
    GO

    Sequence cautioni

    The sequence CAA54388 differs from that shown. Reason: Erroneous initiation.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti18R → A in CAA54388 (PubMed:7980441).Curated1
    Sequence conflicti380R → E AA sequence (PubMed:7935603).Curated1
    Sequence conflicti382H → Q AA sequence (PubMed:7935603).Curated1
    Sequence conflicti387 – 388HS → NP AA sequence (PubMed:7935603).Curated2
    Sequence conflicti482A → R in CAA54388 (PubMed:7980441).Curated1
    Sequence conflicti534T → I in CAA54388 (PubMed:7980441).Curated1
    Sequence conflicti566W → R in CAA54388 (PubMed:7980441).Curated1
    Sequence conflicti739A → G in CAA54388 (PubMed:7980441).Curated1
    Sequence conflicti821K → Q in CAA54388 (PubMed:7980441).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U04863 mRNA. Translation: AAA81906.1.
    X77132 mRNA. Translation: CAA54388.1. Different initiation.
    PIRiS53319.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U04863 mRNA. Translation: AAA81906.1.
    X77132 mRNA. Translation: CAA54388.1. Different initiation.
    PIRiS53319.

    3D structure databases

    ProteinModelPortaliQ24803.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi5759.rna_EHI_150490-1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Phylogenomic databases

    eggNOGiKOG3857. Eukaryota.
    COG1012. LUCA.
    COG1454. LUCA.

    Family and domain databases

    Gene3Di3.40.309.10. 2 hits.
    3.40.605.10. 1 hit.
    InterProiIPR001670. ADH_Fe.
    IPR018211. ADH_Fe_CS.
    IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR012079. Bifunc_Ald-ADH.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    PF00465. Fe-ADH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000111. ALDH_ADH. 1 hit.
    SUPFAMiSSF53720. SSF53720. 2 hits.
    PROSITEiPS00913. ADH_IRON_1. 1 hit.
    PS00060. ADH_IRON_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiADH2_ENTHI
    AccessioniPrimary (citable) accession number: Q24803
    Secondary accession number(s): Q27649
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: September 7, 2016
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing, Multifunctional enzyme

    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.