Q24803 (ADH2_ENTHI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aldehyde-alcohol dehydrogenase 2

Including the following 2 domains:

1. Alcohol dehydrogenase
   Short name=ADH
   EC=1.1.1.1
2. Acetaldehyde dehydrogenase
   Short name=ACDH
   EC=1.2.1.10

Gene names

Name:

ADH2

Organism

Entamoeba histolytica

Taxonomic identifier

5759 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Archamoebae › Entamoebidae › Entamoeba

Protein attributes

Sequence length	870 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme has two NAD+-dependent activities: ADH and ACDH. May be a critical enzyme in the fermentative pathway.
Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH. Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.
Cofactor	Zinc or iron.
Subunit structure	Seems to form a rod shaped homopolymer composed of at least 20 identical subunits.
Sequence similarities	In the N-terminal section; belongs to the aldehyde dehydrogenase family. In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
Sequence caution	The sequence CAA54388.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Ligand	Iron NAD
Molecular function	Oxidoreductase
Technical term	Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological_process	alcohol metabolic process Inferred from electronic annotation. Source: InterPro carbon utilization Inferred from electronic annotation. Source: InterPro
Molecular_function	acetaldehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: EC alcohol dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 870	870	Aldehyde-alcohol dehydrogenase 2		PRO_0000087835
Regions
	Nucleotide binding	431 – 436	6	NAD Potential
	Compositional bias	54 – 59	6	Poly-Ala
Sites
	Active site	252	1	By similarity
Experimental info
	Sequence conflict	18	1	R → A in CAA54388. Ref.2
	Sequence conflict	380	1	R → E AA sequence Ref.1
	Sequence conflict	382	1	H → Q AA sequence Ref.1
	Sequence conflict	387 – 388	2	HS → NP AA sequence Ref.1
	Sequence conflict	482	1	A → R in CAA54388. Ref.2
	Sequence conflict	534	1	T → I in CAA54388. Ref.2
	Sequence conflict	566	1	W → R in CAA54388. Ref.2
	Sequence conflict	739	1	A → G in CAA54388. Ref.2
	Sequence conflict	821	1	K → Q in CAA54388. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q24803 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 66733AD08CE3D0A5	FASTA	870	95,659
	10 20 30 40 50 60 MSTQQTMTVD EHINQLVRKA QVALKEYLKP EYTQEKIDYI VKKASVAALD QHCALAAAAV 70 80 90 100 110 120 EETGRGIFED KATKNIFACE HVTHEMRHAK TVGIINVDPL YGITEIAEPV GVVCGVTPVT 130 140 150 160 170 180 NPTSTAIFKS LISIKTRNPI VFSFHPSALK CSIMAAKIVR DAAIAAGAPE NCIQWIEFGG 190 200 210 220 230 240 IEASNKLMNH PGVATILATG GNAMVKAAYS SGKPALGVGA GNVPTYIEKT CNIKQAANDV 250 260 270 280 290 300 VMSKSFDNGM ICASEQAAII DKEIYDQVVE EMKTLGAYFI NEEEKAKLEK FMFGVNAYSA 310 320 330 340 350 360 DVNNARLNPK CPGMSPQWFA EQVGIKVPED CNIICAVCKE VGPNEPLTRE KLSPVLAILK 370 380 390 400 410 420 AENTQDGIDK AEAMVEFNGR GHSAAIHSND KAVVEKYALT MKACRILHNT PSSQGGIGSI 430 440 450 460 470 480 YNYIWPSFTL GCGSYGGNSV SANVTYHNLL NIKRLADRRN NLQWFRVPPK IFFEPHSIRY 490 500 510 520 530 540 LAELKELSKI FIVSDRMMYK LGYVDRVMDV LKRRSNEVEI EIFIDVEPDP SIQTVQKGLA 550 560 570 580 590 600 VMNTFGPDNI IAIGGGSAMD AAKIMWLLYE HPEADFFAMK QKFIDLRKRA FKFPTMGKKA 610 620 630 640 650 660 RLICIPTTSG TGSEVTPFAV ISDHETGKKY PLADYSLTPS VAIVDPMFTM SLPKRAIADT 670 680 690 700 710 720 GLDVLVHATE AYVSVMANEY TDGLAREAVK LVFENLLKSY NGDLEAREKM HNAATIAGMA 730 740 750 760 770 780 FASAFLGMDH SMAHKVGAAF HLPHGRCVAV LLPHVIRYNG QKPRKLAMWP KYNFYKADQR 790 800 810 820 830 840 YMELAQMVGL KCNTPAEGVE AFAKACEELM KATETITGFK KANIDEAAWM SKVPEMALLA 850 860 870 FEDQCSPANP RVPMVKDMEK ILKAAYYPIA

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U04863 mRNA. Translation: AAA81906.1. X77132 mRNA. Translation: CAA54388.1. Different initiation.
PIR	S53319.
3D structure databases
ProteinModelPortal	Q24803.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG1012.
Family and domain databases
Gene3D	3.40.309.10. 2 hits. 3.40.605.10. 1 hit.
InterPro	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]
Pfam	PF00171. Aldedh. 1 hit. PF00465. Fe-ADH. 1 hit. [Graphical view]
PIRSF	PIRSF000111. ALDH_ADH. 1 hit.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITE	PS00913. ADH_IRON_1. 1 hit. PS00060. ADH_IRON_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADH2_ENTHI

Accession

Primary (citable) accession number: Q24803
Secondary accession number(s): Q27649

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)