ID   ADH_SCHPO               Reviewed;         350 AA.
AC   P00332; Q9URT7;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   02-SEP-2026, entry version 185.
DE   RecName: Full=Alcohol dehydrogenase {ECO:0000305};
DE            EC=1.1.1.1 {ECO:0000305|PubMed:6294096};
GN   Name=adh1; Synonyms=adh; ORFNames=SPCC13B11.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=6294096; DOI=10.1016/s0021-9258(18)33232-0;
RA   Russell P.R., Hall B.D.;
RT   "The primary structure of the alcohol dehydrogenase gene from the fission
RT   yeast Schizosaccharomyces pombe.";
RL   J. Biol. Chem. 258:143-149(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 343-350.
RA   Kawamukai M.;
RT   "S.pombe adh 3' region.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=3546317; DOI=10.1016/s0021-9258(18)61419-x;
RA   Ganzhorn A.J., Green D.W., Hershey A.D., Gould R.M., Plapp B.V.;
RT   "Kinetic characterization of yeast alcohol dehydrogenases. Amino acid
RT   residue 294 and substrate specificity.";
RL   J. Biol. Chem. 262:3754-3761(1987).
RN   [5]
RP   FUNCTION.
RX   PubMed=15040954; DOI=10.1016/j.femsyr.2003.12.009;
RA   Sakurai M., Tohda H., Kumagai H., Giga-Hama Y.;
RT   "A distinct type of alcohol dehydrogenase, adh4+, complements ethanol
RT   fermentation in an adh1-deficient strain of Schizosaccharomyces pombe.";
RL   FEMS Yeast Res. 4:649-654(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND THR-250, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Reduces acetaldehyde to ethanol during the fermentation of
CC       glucose. {ECO:0000269|PubMed:15040954, ECO:0000269|PubMed:3546317}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NAD(+) = an aldehyde + NADH + H(+);
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:0000305|PubMed:6294096};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a secondary alcohol + NAD(+) = a ketone + NADH + H(+);
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:0000305|PubMed:6294096};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ethanol + NAD(+) = acetaldehyde + NADH + H(+);
CC         Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC         Evidence={ECO:0000269|PubMed:3546317};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25291;
CC         Evidence={ECO:0000269|PubMed:3546317};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25292;
CC         Evidence={ECO:0000269|PubMed:3546317};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00330};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=160 uM for NAD(+) {ECO:0000269|PubMed:3546317};
CC         KM=14 mM for ethanol {ECO:0000269|PubMed:3546317};
CC         KM=1.6 mM for acetaldehyde {ECO:0000269|PubMed:3546317};
CC         KM=100 uM for NADH {ECO:0000269|PubMed:3546317};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00330}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00330}.
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; J01341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU329672; CAA21782.1; -; Genomic_DNA.
DR   EMBL; AB001834; BAA19458.1; -; mRNA.
DR   PIR; A00341; DEZPA.
DR   RefSeq; NP_588244.1; NM_001023234.3.
DR   AlphaFoldDB; P00332; -.
DR   SMR; P00332; -.
DR   BioGRID; 275480; 18.
DR   FunCoup; P00332; 411.
DR   STRING; 284812.P00332; -.
DR   iPTMnet; P00332; -.
DR   PaxDb; 284812-P00332; -.
DR   GeneID; 2538902; -.
DR   KEGG; spo:2538902; -.
DR   PomBase; SPCC13B11.01; adh1.
DR   VEuPathDB; FungiDB:SPCC13B11.01; -.
DR   eggNOG; KOG0023; Eukaryota.
DR   HOGENOM; CLU_026673_20_1_1; -.
DR   InParanoid; P00332; -.
DR   OMA; AFPHVKP; -.
DR   PhylomeDB; P00332; -.
DR   PRO; PR:P00332; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IC:PomBase.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR   GO; GO:0120542; F:ethanol dehydrogenase (NAD+) activity; IMP:PomBase.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0019655; P:pyruvate fermentation to ethanol; IGI:PomBase.
DR   CDD; cd08297; CAD3; 1.
DR   FunFam; 3.40.50.720:FF:000039; Alcohol dehydrogenase AdhP; 1.
DR   FunFam; 3.90.180.10:FF:000002; Alcohol dehydrogenase AdhP; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR020843; ER.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42940; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   PANTHER; PTHR42940:SF3; ALCOHOL DEHYDROGENASE 1-RELATED; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW   Reference proteome; Zinc.
FT   CHAIN           1..350
FT                   /note="Alcohol dehydrogenase"
FT                   /id="PRO_0000160729"
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|UniProtKB:P00330"
FT   BINDING         47
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         48
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         51
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         106
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         114
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         156
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         183
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         184
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         204
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         209
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         224
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         271
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         296
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         298
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   BINDING         343
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P00330"
FT   MOD_RES         205
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         250
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   CONFLICT        237
FT                   /note="A -> C (in Ref. 1; J01341)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   350 AA;  37396 MW;  F80BE1341F727CC5 CRC64;
     MTIPDKQLAA VFHTHGGPEN VKFEEVPVAE PGQDEVLVNI KYTGVCHTDL HALQGDWPLP
     AKMPLIGGHE GAGVVVKVGA GVTRLKIGDR VGVKWMNSSC GNCEYCMKAE ETICPHIQLS
     GYTVDGTFQH YCIANATHAT IIPESVPLEV AAPIMCAGIT CYRALKESKV GPGEWICIPG
     AGGGLGHLAV QYAKAMAMRV VAIDTGDDKA ELVKSFGAEV FLDFKKEADM IEAVKAATNG
     GAHGTLVLST SPKSYEQAAG FARPGSTMVT VSMPAGAKLG ADIFWLTVKM LKICGSHVGN
     RIDSIEALEY VSRGLVKPYY KVQPFSTLPD VYRLMHENKI AGRIVLDLSK
//