ADH2_YARLI
ID ADH2_YARLI Reviewed; 351 AA.
AC F2Z678;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Alcohol dehydrogenase 2;
DE EC=1.1.1.1;
GN Name=ADH2; OrderedLocusNames=YALI0E17787g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=CLIB 122 / E 150;
RX DOI=10.3390/biom3030449;
RA Napora-Wijata K., Strohmeier G.A., Sonavane M.N., Avi M., Robins K.,
RA Winkler M.;
RT "Enantiocomplementary Yarrowia lipolytica oxidoreductases: Alcohol
RT dehydrogenase 2 and short chain dehydrogenase/reductase.";
RL Biomolecules 3:449-460(2013).
CC -!- FUNCTION: Versatile oxidoreductase that catalyzes the oxidation and
CC reduction of a broad range of substrates. Preferentially oxidizes
CC secondary alcohols. Has highest activity for racemic 2-octanol. Is also
CC an efficient reductase for selected substrates. Substrate selectivity
CC was found for medium chain lipophilic ketones. Has highest activities
CC for 2-octanone, 2-nonanone and 2-decanone. The enzyme is (S)-selective
CC in the reduction direction and produces exclusively the (S)-enantiomer.
CC {ECO:0000269|Ref.2}.
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|Ref.2};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.42 mM for (S)-2-octanol {ECO:0000269|Ref.2};
CC KM=5.38 mM for (2)-octanone {ECO:0000269|Ref.2};
CC KM=17.8 mM for NAD(+) {ECO:0000269|Ref.2};
CC Note=kcat is 1.05 sec(-1) with (S)-2-octanol as substrate and 3.42
CC sec(-1) for NAD(+). kcat is 0.56 sec(-1) for (2)-octanone.;
CC pH dependence:
CC Optimum pH is 9.5 for the oxidation reaction, and 6.5 for the
CC reduction reaction. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Optimum temperature is 28-33 degrees Celsius. Active from 22 to 37
CC degrees Celsius. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {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; CR382131; CAG79670.1; -; Genomic_DNA.
DR RefSeq; XP_504077.1; XM_504077.1.
DR AlphaFoldDB; F2Z678; -.
DR SMR; F2Z678; -.
DR STRING; 4952.CAG79670; -.
DR PRIDE; F2Z678; -.
DR EnsemblFungi; CAG79670; CAG79670; YALI0_E17787g.
DR GeneID; 2912417; -.
DR KEGG; yli:YALI0E17787g; -.
DR VEuPathDB; FungiDB:YALI0_E17787g; -.
DR HOGENOM; CLU_026673_20_1_1; -.
DR InParanoid; F2Z678; -.
DR OMA; GLKMTDT; -.
DR Proteomes; UP000001300; Chromosome E.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR InterPro; IPR013149; ADH-like_C.
DR InterPro; IPR013154; ADH_N.
DR InterPro; IPR002328; ADH_Zn_CS.
DR InterPro; IPR011032; GroES-like_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020843; PKS_ER.
DR Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SMART; SM00829; PKS_ER; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..351
FT /note="Alcohol dehydrogenase 2"
FT /id="PRO_0000425281"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 181..187
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 205
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 272..274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 351 AA; 37315 MW; FD626D7D5EAF133B CRC64;
MSAPVIPKTQ KGVIFETSGG PLMYKDIPVP VPADDEILVN VKFSGVCHTD LHAWKGDWPL
DTKLPLVGGH EGAGVVVAKG KNVDTFEIGD YAGIKWINKA CYTCEFCQVA AEPNCPNATM
SGYTHDGSFQ QYATANAVQA AHIPKNCDLA EIAPILCAGI TVYKALKTAA ILAGQWVAVT
GAGGGLGTLA VQYAKAMGYR VLAIDTGADK EKMCKDLGAE VFIDFAKTKD LVKDVQEATK
GGPHAVINVS VSEFAVNQSI EYVRTLGTVV LVGLPAGAVC KSPIFQQVAR SIQIKGSYVG
NRADSQEAIE FFSRGLVKSP IIIIGLSELE KVYKLMEEGK IAGRYVLDTS K
