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Q24803

- ADH2_ENTHI

UniProt

Q24803 - ADH2_ENTHI

Protein

Aldehyde-alcohol dehydrogenase 2

Gene

ADH2

Organism
Entamoeba histolytica
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    Zinc or iron.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei252 – 2521By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi431 – 4366NADSequence Analysis

    GO - Molecular functioni

    1. acetaldehyde dehydrogenase (acetylating) activity Source: UniProtKB-EC
    2. alcohol dehydrogenase (NAD) activity Source: UniProtKB-EC
    3. metal ion binding Source: InterPro

    GO - Biological processi

    1. alcohol metabolic process Source: InterPro
    2. carbon utilization Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Iron, NAD

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde-alcohol dehydrogenase 2
    Including the following 2 domains:
    Alcohol dehydrogenase (EC:1.1.1.1)
    Short name:
    ADH
    Acetaldehyde dehydrogenase (EC:1.2.1.10)
    Short name:
    ACDH
    Gene namesi
    Name:ADH2
    OrganismiEntamoeba histolytica
    Taxonomic identifieri5759 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaArchamoebaeEntamoebidaeEntamoeba

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 870870Aldehyde-alcohol dehydrogenase 2PRO_0000087835Add
    BLAST

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ24803.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi54 – 596Poly-Ala

    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

    eggNOGiCOG1012.

    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

    MSTQQTMTVD EHINQLVRKA QVALKEYLKP EYTQEKIDYI VKKASVAALD    50
    QHCALAAAAV EETGRGIFED KATKNIFACE HVTHEMRHAK TVGIINVDPL 100
    YGITEIAEPV GVVCGVTPVT NPTSTAIFKS LISIKTRNPI VFSFHPSALK 150
    CSIMAAKIVR DAAIAAGAPE NCIQWIEFGG IEASNKLMNH PGVATILATG 200
    GNAMVKAAYS SGKPALGVGA GNVPTYIEKT CNIKQAANDV VMSKSFDNGM 250
    ICASEQAAII DKEIYDQVVE EMKTLGAYFI NEEEKAKLEK FMFGVNAYSA 300
    DVNNARLNPK CPGMSPQWFA EQVGIKVPED CNIICAVCKE VGPNEPLTRE 350
    KLSPVLAILK AENTQDGIDK AEAMVEFNGR GHSAAIHSND KAVVEKYALT 400
    MKACRILHNT PSSQGGIGSI YNYIWPSFTL GCGSYGGNSV SANVTYHNLL 450
    NIKRLADRRN NLQWFRVPPK IFFEPHSIRY LAELKELSKI FIVSDRMMYK 500
    LGYVDRVMDV LKRRSNEVEI EIFIDVEPDP SIQTVQKGLA VMNTFGPDNI 550
    IAIGGGSAMD AAKIMWLLYE HPEADFFAMK QKFIDLRKRA FKFPTMGKKA 600
    RLICIPTTSG TGSEVTPFAV ISDHETGKKY PLADYSLTPS VAIVDPMFTM 650
    SLPKRAIADT GLDVLVHATE AYVSVMANEY TDGLAREAVK LVFENLLKSY 700
    NGDLEAREKM HNAATIAGMA FASAFLGMDH SMAHKVGAAF HLPHGRCVAV 750
    LLPHVIRYNG QKPRKLAMWP KYNFYKADQR YMELAQMVGL KCNTPAEGVE 800
    AFAKACEELM KATETITGFK KANIDEAAWM SKVPEMALLA FEDQCSPANP 850
    RVPMVKDMEK ILKAAYYPIA 870
    Length:870
    Mass (Da):95,659
    Last modified:November 1, 1997 - v1
    Checksum:i66733AD08CE3D0A5
    GO

    Sequence cautioni

    The sequence CAA54388.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181R → A in CAA54388. (PubMed:7980441)Curated
    Sequence conflicti380 – 3801R → E AA sequence (PubMed:7935603)Curated
    Sequence conflicti382 – 3821H → Q AA sequence (PubMed:7935603)Curated
    Sequence conflicti387 – 3882HS → NP AA sequence (PubMed:7935603)Curated
    Sequence conflicti482 – 4821A → R in CAA54388. (PubMed:7980441)Curated
    Sequence conflicti534 – 5341T → I in CAA54388. (PubMed:7980441)Curated
    Sequence conflicti566 – 5661W → R in CAA54388. (PubMed:7980441)Curated
    Sequence conflicti739 – 7391A → G in CAA54388. (PubMed:7980441)Curated
    Sequence conflicti821 – 8211K → Q in CAA54388. (PubMed:7980441)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04863 mRNA. Translation: AAA81906.1.
    X77132 mRNA. Translation: CAA54388.1. Different initiation.
    PIRiS53319.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U04863 mRNA. Translation: AAA81906.1 .
    X77132 mRNA. Translation: CAA54388.1 . Different initiation.
    PIRi S53319.

    3D structure databases

    ProteinModelPortali Q24803.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG1012.

    Family and domain databases

    Gene3Di 3.40.309.10. 2 hits.
    3.40.605.10. 1 hit.
    InterProi IPR001670. 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 ]
    Pfami PF00171. Aldedh. 1 hit.
    PF00465. Fe-ADH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000111. ALDH_ADH. 1 hit.
    SUPFAMi SSF53720. SSF53720. 2 hits.
    PROSITEi PS00913. ADH_IRON_1. 1 hit.
    PS00060. ADH_IRON_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli."
      Yang W., Li E., Kairong T., Stanley S.L. Jr.
      Mol. Biochem. Parasitol. 64:253-260(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 377-395 AND 860-870.
      Strain: ATCC 30459 / HM-1:IMSS.
    2. "Purification and molecular characterization of the NAD(+)-dependent acetaldehyde/alcohol dehydrogenase from Entamoeba histolytica."
      Bruchhaus I., Tannich E.
      Biochem. J. 303:743-748(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: ATCC 30459 / HM-1:IMSS.

    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: October 1, 2014
    This is version 72 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

    External Data

    Dasty 3