ADH4_SCHPO
ID ADH4_SCHPO Reviewed; 422 AA.
AC Q09669;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Alcohol dehydrogenase 4;
DE EC=1.1.1.1 {ECO:0000269|PubMed:15040954, ECO:0000269|PubMed:16999687};
DE AltName: Full=Alcohol dehydrogenase IV;
DE Flags: Precursor;
GN Name=adh4; ORFNames=SPAC5H10.06c;
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 [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 [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=16999687; DOI=10.1042/bj20061181;
RA Crichton P.G., Affourtit C., Moore A.L.;
RT "Identification of a mitochondrial alcohol dehydrogenase in
RT Schizosaccharomyces pombe: new insights into energy metabolism.";
RL Biochem. J. 401:459-464(2007).
RN [5]
RP INDUCTION.
RX PubMed=18203864; DOI=10.1128/ec.00408-07;
RA Dainty S.J., Kennedy C.A., Watt S., Baehler J., Whitehall S.K.;
RT "Response of Schizosaccharomyces pombe to zinc deficiency.";
RL Eukaryot. Cell 7:454-464(2008).
CC -!- FUNCTION: Involved in ethanol oxidation in mitochondria.
CC {ECO:0000269|PubMed:15040954, ECO:0000269|PubMed:16999687}.
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:15040954, ECO:0000269|PubMed:16999687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10737;
CC Evidence={ECO:0000269|PubMed:16999687};
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:0000305|PubMed:15040954, ECO:0000305|PubMed:16999687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10741;
CC Evidence={ECO:0000305|PubMed:16999687};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16999687}.
CC -!- INDUCTION: Induced in response to zinc deficiency.
CC {ECO:0000269|PubMed:18203864}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; CU329670; CAA89956.1; -; Genomic_DNA.
DR PIR; S55484; S55484.
DR RefSeq; NP_592819.1; NM_001018219.2.
DR AlphaFoldDB; Q09669; -.
DR SMR; Q09669; -.
DR BioGRID; 279167; 24.
DR STRING; 4896.SPAC5H10.06c.1; -.
DR MaxQB; Q09669; -.
DR PaxDb; Q09669; -.
DR GeneID; 2542714; -.
DR KEGG; spo:SPAC5H10.06c; -.
DR PomBase; SPAC5H10.06c; adh4.
DR eggNOG; KOG3857; Eukaryota.
DR InParanoid; Q09669; -.
DR OMA; LPHTAHY; -.
DR PhylomeDB; Q09669; -.
DR BRENDA; 1.1.1.1; 5613.
DR PRO; PR:Q09669; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IMP:PomBase.
DR GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043458; P:ethanol biosynthetic process involved in glucose fermentation to ethanol; IGI:PomBase.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Mitochondrion; NAD; Oxidoreductase; Reference proteome;
KW Transit peptide; Zinc.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..422
FT /note="Alcohol dehydrogenase 4"
FT /id="PRO_0000087818"
SQ SEQUENCE 422 AA; 45527 MW; C70B56632DBC658E CRC64;
MSILRSPFRL IRSPARFFPS LFHSSCNQSF TNGLKHQSTS SKAMPVSAFY IPSFNLFGKG
CLAEAAKQIK MSGFKNTLIV TDPGIIKVGL YDKVKALLEE QSITVHLYDG VQPNPTVGNV
NQGLEIVKKE NCDSMVSIGG GSAHDCAKGI ALLATNGGKI ADYEGVDKSS KPQLPLIAIN
TTAGTASEMT RFAIITEETR HIKMAIIDKH TMPILSVNDP ETMYGLPPSL TAATGMDALT
HAVEAYVSTA ANPITDACAV KCIELVNKYL KRAVDNGKDE EARDNMAYAE FLGGMAFNNA
SLGYVHAMAH QLGGFYGIPH GVCNAVLLAH VQKFNSRDPR ANARLGDIAF HLGCEEHTAE
AALDRISQLV LEVKIRPHLV DLGVKEKDFD VLVDHAMKDA CGATNPIQPT HDEVKAIFKS
AM
