ADH6_YEAST
ID ADH6_YEAST Reviewed; 360 AA.
AC Q04894; D6W0E6;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=NADP-dependent alcohol dehydrogenase 6;
DE EC=1.1.1.2;
DE AltName: Full=NADP-dependent alcohol dehydrogenase VI;
DE AltName: Full=ScADHVI;
GN Name=ADH6; OrderedLocusNames=YMR318C; ORFNames=YM9924.10C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP CRYSTALLIZATION.
RX PubMed=12554944; DOI=10.1107/s090744490201661x;
RA Valencia E., Rosell A., Larroy C., Farres J., Biosca J.A., Fita I.,
RA Pares X., Ochoa W.F.;
RT "Crystallization and preliminary X-ray analysis of NADP(H)-dependent
RT alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi.";
RL Acta Crystallogr. D 59:334-337(2003).
RN [4]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-359, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: NADP-dependent alcohol dehydrogenase with a broad substrate
CC specificity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2;
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 -!- MISCELLANEOUS: Present with 21700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; Z54141; CAA90836.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10220.1; -; Genomic_DNA.
DR PIR; S59311; S59311.
DR RefSeq; NP_014051.3; NM_001182831.3.
DR PDB; 1PIW; X-ray; 3.00 A; A/B=1-360.
DR PDB; 1PS0; X-ray; 3.01 A; A=1-360.
DR PDB; 1Q1N; X-ray; 3.15 A; A=1-360.
DR PDBsum; 1PIW; -.
DR PDBsum; 1PS0; -.
DR PDBsum; 1Q1N; -.
DR AlphaFoldDB; Q04894; -.
DR SMR; Q04894; -.
DR BioGRID; 35498; 84.
DR DIP; DIP-6308N; -.
DR IntAct; Q04894; 4.
DR STRING; 4932.YMR318C; -.
DR iPTMnet; Q04894; -.
DR MaxQB; Q04894; -.
DR PaxDb; Q04894; -.
DR PRIDE; Q04894; -.
DR EnsemblFungi; YMR318C_mRNA; YMR318C; YMR318C.
DR GeneID; 855368; -.
DR KEGG; sce:YMR318C; -.
DR SGD; S000004937; ADH6.
DR VEuPathDB; FungiDB:YMR318C; -.
DR eggNOG; KOG0023; Eukaryota.
DR GeneTree; ENSGT00940000176642; -.
DR HOGENOM; CLU_026673_20_2_1; -.
DR InParanoid; Q04894; -.
DR OMA; DNETYCQ; -.
DR BioCyc; YEAST:YMR318C-MON; -.
DR SABIO-RK; Q04894; -.
DR EvolutionaryTrace; Q04894; -.
DR PRO; PR:Q04894; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04894; protein.
DR GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:SGD.
DR GO; GO:0033833; F:hydroxymethylfurfural reductase (NADH) activity; IMP:SGD.
DR GO; GO:0033845; F:hydroxymethylfurfural reductase (NADPH) activity; IMP:SGD.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006066; P:alcohol metabolic process; IDA:SGD.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IDA:SGD.
DR GO; GO:0033859; P:furaldehyde metabolic process; IMP:SGD.
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 Pfam; PF08240; ADH_N; 1.
DR Pfam; PF00107; ADH_zinc_N; 1.
DR SUPFAM; SSF50129; SSF50129; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00059; ADH_ZINC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Zinc.
FT CHAIN 1..360
FT /note="NADP-dependent alcohol dehydrogenase 6"
FT /id="PRO_0000160734"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 187..192
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 275..277
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT TURN 3..5
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 7..12
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 35..45
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:1PIW"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1Q1N"
FT HELIX 104..107
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 134..142
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1PS0"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 295..298
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:1PIW"
FT STRAND 346..352
FT /evidence="ECO:0007829|PDB:1PIW"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:1PIW"
SQ SEQUENCE 360 AA; 39618 MW; 3F785BE0C5ED8CF1 CRC64;
MSYPEKFEGI AIQSHEDWKN PKKTKYDPKP FYDHDIDIKI EACGVCGSDI HCAAGHWGNM
KMPLVVGHEI VGKVVKLGPK SNSGLKVGQR VGVGAQVFSC LECDRCKNDN EPYCTKFVTT
YSQPYEDGYV SQGGYANYVR VHEHFVVPIP ENIPSHLAAP LLCGGLTVYS PLVRNGCGPG
KKVGIVGLGG IGSMGTLISK AMGAETYVIS RSSRKREDAM KMGADHYIAT LEEGDWGEKY
FDTFDLIVVC ASSLTDIDFN IMPKAMKVGG RIVSISIPEQ HEMLSLKPYG LKAVSISYSA
LGSIKELNQL LKLVSEKDIK IWVETLPVGE AGVHEAFERM EKGDVRYRFT LVGYDKEFSD
