ADH_SCHPO
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 03-AUG-2022, entry version 171.
DE RecName: Full=Alcohol dehydrogenase;
DE EC=1.1.1.1;
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].
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 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 -!- 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 -!- 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Note=Binds 2 Zn(2+) ions per subunit.;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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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_001023234.2.
DR AlphaFoldDB; P00332; -.
DR SMR; P00332; -.
DR BioGRID; 275480; 13.
DR STRING; 4896.SPCC13B11.01.1; -.
DR iPTMnet; P00332; -.
DR MaxQB; P00332; -.
DR PaxDb; P00332; -.
DR PRIDE; P00332; -.
DR EnsemblFungi; SPCC13B11.01.1; SPCC13B11.01.1:pep; SPCC13B11.01.
DR GeneID; 2538902; -.
DR KEGG; spo:SPCC13B11.01; -.
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; EIGGQCG; -.
DR PhylomeDB; P00332; -.
DR PRO; PR:P00332; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IMP:PomBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043458; P:ethanol biosynthetic process involved in glucose fermentation to ethanol; IGI:PomBase.
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 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 BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 180..186
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 271..273
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
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
