Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q24803

- ADH2_ENTHI

UniProt

Q24803 - ADH2_ENTHI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

Zn2+, Fe2+Note: 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
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.
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

        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 CAA54388.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
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.
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: November 26, 2014
This is version 73 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