ADH2_ENTHI
ID ADH2_ENTHI Reviewed; 870 AA.
AC Q24803; Q27649;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Aldehyde-alcohol dehydrogenase 2 {ECO:0000305};
DE Includes:
DE RecName: Full=Alcohol dehydrogenase {ECO:0000303|PubMed:7935603, ECO:0000303|PubMed:7980441};
DE Short=ADH {ECO:0000303|PubMed:7935603, ECO:0000303|PubMed:7980441};
DE EC=1.1.1.1 {ECO:0000269|PubMed:7935603, ECO:0000269|PubMed:7980441};
DE Includes:
DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000303|PubMed:7935603, ECO:0000303|PubMed:7980441};
DE Short=ACDH {ECO:0000303|PubMed:7980441};
DE EC=1.2.1.10 {ECO:0000269|PubMed:7935603, ECO:0000269|PubMed:7980441};
GN Name=ADH2;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 377-395 AND 860-870,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=7935603; DOI=10.1016/0166-6851(93)00020-a;
RA Yang W., Li E., Kairong T., Stanley S.L. Jr.;
RT "Entamoeba histolytica has an alcohol dehydrogenase homologous to the
RT multifunctional adhE gene product of Escherichia coli.";
RL Mol. Biochem. Parasitol. 64:253-260(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=7980441; DOI=10.1042/bj3030743;
RA Bruchhaus I., Tannich E.;
RT "Purification and molecular characterization of the NAD(+)-dependent
RT acetaldehyde/alcohol dehydrogenase from Entamoeba histolytica.";
RL Biochem. J. 303:743-748(1994).
CC -!- FUNCTION: This enzyme has two NAD(+)-dependent activities: ADH and
CC ACDH. May be a critical enzyme in the fermentative pathway.
CC {ECO:0000269|PubMed:7935603, ECO:0000269|PubMed:7980441}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:7935603, ECO:0000269|PubMed:7980441};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH;
CC Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087,
CC ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000269|PubMed:7935603, ECO:0000269|PubMed:7980441};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.10; Evidence={ECO:0000269|PubMed:7935603,
CC ECO:0000269|PubMed:7980441};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Zinc or iron. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80 mM for ethanol {ECO:0000269|PubMed:7980441};
CC KM=0.15 mM for acetaldehyde {ECO:0000269|PubMed:7980441};
CC KM=0.015 mM for acetyl-CoA {ECO:0000269|PubMed:7980441};
CC KM=0.15 mM for NAD(+) (for ADH activity)
CC {ECO:0000269|PubMed:7980441};
CC KM=0.05 mM for NADH (for ADH activity) {ECO:0000269|PubMed:7980441};
CC KM=0.18 mM for NADH (for ACDH activity) {ECO:0000269|PubMed:7980441};
CC -!- SUBUNIT: Seems to form a rod shaped homomer composed of at least 20
CC identical subunits. {ECO:0000269|PubMed:7980441}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC alcohol dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA54388.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U04863; AAA81906.1; -; mRNA.
DR EMBL; X77132; CAA54388.1; ALT_INIT; mRNA.
DR PIR; S53319; S53319.
DR AlphaFoldDB; Q24803; -.
DR SMR; Q24803; -.
DR STRING; 5759.rna_EHI_150490-1; -.
DR MoonProt; Q24803; -.
DR PRIDE; Q24803; -.
DR VEuPathDB; AmoebaDB:EHI5A_157720; -.
DR VEuPathDB; AmoebaDB:EHI7A_198850; -.
DR VEuPathDB; AmoebaDB:EHI8A_086570; -.
DR VEuPathDB; AmoebaDB:EHI_160940; -.
DR VEuPathDB; AmoebaDB:KM1_283380; -.
DR eggNOG; KOG3857; Eukaryota.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IDA:CAFA.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IDA:CAFA.
DR GO; GO:0005518; F:collagen binding; IDA:CAFA.
DR GO; GO:0001968; F:fibronectin binding; IDA:CAFA.
DR GO; GO:0043236; F:laminin binding; IDA:CAFA.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd08178; AAD_C; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR034789; AAD_C.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012079; Bifunc_Ald-ADH.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000111; ALDH_ADH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Iron; Multifunctional enzyme; NAD;
KW Oxidoreductase.
FT CHAIN 1..870
FT /note="Aldehyde-alcohol dehydrogenase 2"
FT /id="PRO_0000087835"
FT ACT_SITE 252
FT /evidence="ECO:0000250"
FT BINDING 431..436
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT CONFLICT 18
FT /note="R -> A (in Ref. 2; CAA54388)"
FT /evidence="ECO:0000305"
FT CONFLICT 380
FT /note="R -> E (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="H -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 387..388
FT /note="HS -> NP (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="A -> R (in Ref. 2; CAA54388)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="T -> I (in Ref. 2; CAA54388)"
FT /evidence="ECO:0000305"
FT CONFLICT 566
FT /note="W -> R (in Ref. 2; CAA54388)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="A -> G (in Ref. 2; CAA54388)"
FT /evidence="ECO:0000305"
FT CONFLICT 821
FT /note="K -> Q (in Ref. 2; CAA54388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 95659 MW; 66733AD08CE3D0A5 CRC64;
MSTQQTMTVD EHINQLVRKA QVALKEYLKP EYTQEKIDYI VKKASVAALD QHCALAAAAV
EETGRGIFED KATKNIFACE HVTHEMRHAK TVGIINVDPL YGITEIAEPV GVVCGVTPVT
NPTSTAIFKS LISIKTRNPI VFSFHPSALK CSIMAAKIVR DAAIAAGAPE NCIQWIEFGG
IEASNKLMNH PGVATILATG GNAMVKAAYS SGKPALGVGA GNVPTYIEKT CNIKQAANDV
VMSKSFDNGM ICASEQAAII DKEIYDQVVE EMKTLGAYFI NEEEKAKLEK FMFGVNAYSA
DVNNARLNPK CPGMSPQWFA EQVGIKVPED CNIICAVCKE VGPNEPLTRE KLSPVLAILK
AENTQDGIDK AEAMVEFNGR GHSAAIHSND KAVVEKYALT MKACRILHNT PSSQGGIGSI
YNYIWPSFTL GCGSYGGNSV SANVTYHNLL NIKRLADRRN NLQWFRVPPK IFFEPHSIRY
LAELKELSKI FIVSDRMMYK LGYVDRVMDV LKRRSNEVEI EIFIDVEPDP SIQTVQKGLA
VMNTFGPDNI IAIGGGSAMD AAKIMWLLYE HPEADFFAMK QKFIDLRKRA FKFPTMGKKA
RLICIPTTSG TGSEVTPFAV ISDHETGKKY PLADYSLTPS VAIVDPMFTM SLPKRAIADT
GLDVLVHATE AYVSVMANEY TDGLAREAVK LVFENLLKSY NGDLEAREKM HNAATIAGMA
FASAFLGMDH SMAHKVGAAF HLPHGRCVAV LLPHVIRYNG QKPRKLAMWP KYNFYKADQR
YMELAQMVGL KCNTPAEGVE AFAKACEELM KATETITGFK KANIDEAAWM SKVPEMALLA
FEDQCSPANP RVPMVKDMEK ILKAAYYPIA
