DSF1_YEAST
ID DSF1_YEAST Reviewed; 502 AA.
AC P0CX08; D3DLI1; P39941;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Mannitol dehydrogenase DSF1 {ECO:0000303|PubMed:26996892};
DE EC=1.1.1.67 {ECO:0000269|PubMed:26996892};
DE AltName: Full=Deletion suppressor of MPT5 mutation protein 1 {ECO:0000303|PubMed:16328373};
GN Name=DSF1 {ECO:0000303|PubMed:16328373};
GN Synonyms=MAN1 {ECO:0000303|PubMed:26996892}; OrderedLocusNames=YEL070W;
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=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=16328373; DOI=10.1007/s00438-005-0064-x;
RA Ohkuni K., Kikuchi Y., Hara K., Taneda T., Hayashi N., Kikuchi A.;
RT "Suppressor analysis of the mpt5/htr1/uth4/puf5 deletion in Saccharomyces
RT cerevisiae.";
RL Mol. Genet. Genomics 275:81-88(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26996892; DOI=10.1038/srep23502;
RA Jordan P., Choe J.Y., Boles E., Oreb M.;
RT "Hxt13, Hxt15, Hxt16 and Hxt17 from Saccharomyces cerevisiae represent a
RT novel type of polyol transporters.";
RL Sci. Rep. 6:23502-23502(2016).
CC -!- FUNCTION: Catalyzes the NAD(H)-dependent interconversion of D-fructose
CC and D-mannitol in the mannitol metabolic pathway.
CC {ECO:0000269|PubMed:26996892}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol + NAD(+) = D-fructose + H(+) + NADH;
CC Xref=Rhea:RHEA:12084, ChEBI:CHEBI:15378, ChEBI:CHEBI:16899,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.67;
CC Evidence={ECO:0000269|PubMed:26996892};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.9 mM for mannitol {ECO:0000269|PubMed:26996892};
CC KM=869.6 mM for sorbitol {ECO:0000269|PubMed:26996892};
CC Vmax=0.1 umol/min/mg enzyme toward mannitol
CC {ECO:0000269|PubMed:26996892};
CC Vmax=1.5 umol/min/mg enzyme toward sorbitol
CC {ECO:0000269|PubMed:26996892};
CC -!- DISRUPTION PHENOTYPE: Rescues temperature-sensitivity of MPT5 deletion.
CC {ECO:0000269|PubMed:16328373}.
CC -!- MISCELLANEOUS: There are two genes for this mannitol dehydrogenase in
CC yeast, DSF1 and YNR073C.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; U18795; AAB65017.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07585.1; -; Genomic_DNA.
DR PIR; S50519; S50519.
DR RefSeq; NP_010844.1; NM_001178885.1.
DR RefSeq; NP_014471.3; NM_001183250.3.
DR AlphaFoldDB; P0CX08; -.
DR SMR; P0CX08; -.
DR BioGRID; 35899; 81.
DR BioGRID; 36661; 56.
DR STRING; 4932.YEL070W; -.
DR PaxDb; P0CX08; -.
DR PRIDE; P0CX08; -.
DR TopDownProteomics; P0CX08; -.
DR EnsemblFungi; YEL070W_mRNA; YEL070W; YEL070W.
DR EnsemblFungi; YNR073C_mRNA; YNR073C; YNR073C.
DR GeneID; 855810; -.
DR GeneID; 856639; -.
DR KEGG; sce:YEL070W; -.
DR KEGG; sce:YNR073C; -.
DR SGD; S000000796; DSF1.
DR VEuPathDB; FungiDB:YEL070W; -.
DR VEuPathDB; FungiDB:YNR073C; -.
DR eggNOG; ENOG502QT30; Eukaryota.
DR HOGENOM; CLU_027324_0_1_1; -.
DR InParanoid; P0CX08; -.
DR OMA; YKPYDNL; -.
DR BioCyc; YEAST:G3O-30185-MON; -.
DR PRO; PR:P0CX08; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P0CX08; protein.
DR ExpressionAtlas; P0CX08; baseline and differential.
DR GO; GO:0050086; F:mannitol 2-dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046029; F:mannitol dehydrogenase 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:0019594; P:mannitol metabolic process; IEA:InterPro.
DR Gene3D; 1.10.1040.10; -; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR000669; Mannitol_DH.
DR InterPro; IPR013118; Mannitol_DH_C.
DR InterPro; IPR023027; Mannitol_DH_CS.
DR InterPro; IPR013131; Mannitol_DH_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01232; Mannitol_dh; 1.
DR Pfam; PF08125; Mannitol_dh_C; 1.
DR PRINTS; PR00084; MTLDHDRGNASE.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00974; MANNITOL_DHGENASE; 1.
PE 1: Evidence at protein level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..502
FT /note="Mannitol dehydrogenase DSF1"
FT /id="PRO_0000170751"
SQ SEQUENCE 502 AA; 56470 MW; A7E0CC01AADC1B2A CRC64;
MTKSDETTAT SLNAKTLKSF ESTLPIPTYP REGVKQGIVH LGVGAFHRSH LAVFMHRLMQ
EHHLKDWSIC GVGLMKADAL MRDAMKAQDC LYTLVERGIK DTNAYIVGSI TAYMYAPDDP
RAVIEKMANP DTHIVSLTVT ENGYYHSEAT NSLMTDAPEI INDLNHPEKP DTLYGYLYEA
LLLRYKRGLT PFTIMSCDNM PQNGVTVKTM LVAFAKLKKD EKFAAWIEDK VTSPNSMVDR
VTPRCTDKER KYVADTWGIK DQCPVVAEPF IQWVLEDNFS DGRPPWELVG VQVVKDVDSY
ELMKLRLLNG GHSAMGYLGY LAGYTYIHEV VNDPTINKYI RVLMREEVIP LLPKVPGVDF
EEYTASVLER FSNPAIQDTV ARICLMGSGK MPKYVLPSIY EQLRKPDGKY KLLAVCVAGW
FRYLTGVDMN GKPFEIEDPM APTLKAAAVK GGKDPHELLN IEVLFSPEIR DNKEFVAQLT
HSLETVYDKG PIAAIKEILD QV
