| General Information |
| MoonProt ID | 15 |
| First appeared in release | 1.0 |
| Name(s) | alcohol dehydrogenase (EhADH2)
ADH
ACDH
Aldehyde-alcohol dehydrogenase 2
Gene name = ADH2
Has two enzyme domains
Alcohol dehydrogenase
Acetaldehyde dehydrogenase
|
| UniProt ID | Q24803 (ADH2_ENTHI), Reviewed |
| GO terms | GO:0006066 alcohol metabolic process
GO:0008152 metabolic process
GO:0015976 carbon utilization
GO:0055114 oxidation-reduction process
GO:0003824 catalytic activity
GO:0004022 alcohol dehydrogenase (NAD) activity
GO:0008774 acetaldehyde dehydrogenase (acetylating) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
|
| Organisms for which functions have been demonstrated | Enteamoeba histolytica (amoeba, anaerobic eukaryote) |
| Sequence length | 870 |
| FASTA sequence | >gi|2492737|sp|Q24803.1|ADH2_ENTHI RecName: Full=Aldehyde-alcohol dehydrogenase 2; Includes: RecName: Full=Alcohol dehydrogenase; Short=ADH; Includes: RecName: Full=Acetaldehyde dehydrogenase; Short=ACDH
MSTQQTMTVDEHINQLVRKAQVALKEYLKPEYTQEKIDYIVKKASVAALDQHCALAAAAVEETGRGIFEDKATKNIFACEHVTHEMRHAKTVGIINVDPLYGITEIAEPVGVVCGVTPVTNPTSTAIFKSLISIKTRNPIVFSFHPSALKCSIMAAKIVRDAAIAAGAPENCIQWIEFGGIEASNKLMNHPGVATILATGGNAMVKAAYSSGKPALGVGAGNVPTYIEKTCNIKQAANDVVMSKSFDNGMICASEQAAIIDKEIYDQVVEEMKTLGAYFINEEEKAKLEKFMFGVNAYSADVNNARLNPKCPGMSPQWFAEQVGIKVPEDCNIICAVCKEVGPNEPLTREKLSPVLAILKAENTQDGIDKAEAMVEFNGRGHSAAIHSNDKAVVEKYALTMKACRILHNTPSSQGGIGSIYNYIWPSFTLGCGSYGGNSVSANVTYHNLLNIKRLADRRNNLQWFRVPPKIFFEPHSIRYLAELKELSKIFIVSDRMMYKLGYVDRVMDVLKRRSNEVEIEIFIDVEPDPSIQTVQKGLAVMNTFGPDNIIAIGGGSAMDAAKIMWLLYEHPEADFFAMKQKFIDLRKRAFKFPTMGKKARLICIPTTSGTGSEVTPFAVISDHETGKKYPLADYSLTPSVAIVDPMFTMSLPKRAIADTGLDVLVHATEAYVSVMANEYTDGLAREAVKLVFENLLKSYNGDLEAREKMHNAATIAGMAFASAFLGMDHSMAHKVGAAFHLPHGRCVAVLLPHVIRYNGQKPRKLAMWPKYNFYKADQRYMELAQMVGLKCNTPAEGVEAFAKACEELMKATETITGFKKANIDEAAWMSKVPEMALLAFEDQCSPANPRVPMVKDMEKILKAAYYPIA |
| Structure Information |
| PDB ID | Closest homologue is 6AHC with 46.44% amino acid sequence identity |
| Quaternary structure | |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 1--12, 869-870 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | alcohol dehydrogenase (EhADH2), enzyme
Including the following 2 domains: Alcohol dehydrogenase and Acetaldehyde dehydrogenase
An alcohol + NAD+ => an aldehyde or ketone + NADH
Acetaldehyde + CoA + NAD+ => acetyl-CoA + NADH.
demonstrated that it has both ADH and acetaldehyde dehydrogenase activity. |
| References for function | Yang W, Li E, Kairong T, Stanley SL Jr. Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli. Mol Biochem Parasitol. 1994 Apr;64(2):253-60. PMID: 7935603. |
| E.C. number | Has two enzyme domains: EC=1.1.1.1 and EC=1.2.1.10 |
| Location of functional site(s) | |
| Cellular location of function | cytoplasm |
| Comments | |
| Function 2 |
| Function description | binds fibronectin, laminin, and type II collagen
|
| References for function | Yang W, Li E, Kairong T, Stanley SL Jr. Entamoeba histolytica has an alcohol dehydrogenase homologous to the multifunctional adhE gene product of Escherichia coli. Mol Biochem Parasitol. 1994 Apr;64(2):253-60. PMID: 7935603. |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | cell surface |
| Comments | |