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Q24803

- ADH2_ENTHI

UniProt

Q24803 - ADH2_ENTHI

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Protein

Aldehyde-alcohol dehydrogenase 2

Gene
ADH2
Organism
Entamoeba histolytica
Status
Reviewed - Annotation score: 4 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.

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 – 2521 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi431 – 4366NAD Reviewed prediction

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
Complete GO annotation...

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.

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

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181R → A in CAA54388. 1 Publication
Sequence conflicti380 – 3801R → E AA sequence 1 Publication
Sequence conflicti382 – 3821H → Q AA sequence 1 Publication
Sequence conflicti387 – 3882HS → NP AA sequence 1 Publication
Sequence conflicti482 – 4821A → R in CAA54388. 1 Publication
Sequence conflicti534 – 5341T → I in CAA54388. 1 Publication
Sequence conflicti566 – 5661W → R in CAA54388. 1 Publication
Sequence conflicti739 – 7391A → G in CAA54388. 1 Publication
Sequence conflicti821 – 8211K → Q in CAA54388. 1 Publication

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: September 3, 2014
This is version 71 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

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