MAN2_YEAST
ID MAN2_YEAST Reviewed; 502 AA.
AC P0CX09; D3DLI1; P39941;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Mannitol dehydrogenase 2 {ECO:0000303|PubMed:26996892};
DE EC=1.1.1.67 {ECO:0000269|PubMed:26996892};
GN Name=MAN2 {ECO:0000303|PubMed:26996892}; OrderedLocusNames=YNR073C;
GN ORFNames=N3810;
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=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-439.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8904342;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<289::aid-yea909>3.0.co;2-m;
RA Levesque H., Lepingle A., Nicaud J.-M., Gaillardin C.;
RT "Sequencing of a 9.2 kb telomeric fragment from the right arm of
RT Saccharomyces cerevisiae chromosome XIV.";
RL Yeast 12:289-295(1996).
RN [4]
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=3.6 mM for mannitol {ECO:0000269|PubMed:26996892};
CC KM=634.9 mM for sorbitol {ECO:0000269|PubMed:26996892};
CC Vmax=0.4 umol/min/mg enzyme toward mannitol
CC {ECO:0000269|PubMed:26996892};
CC Vmax=2.1 umol/min/mg enzyme toward sorbitol
CC {ECO:0000269|PubMed:26996892};
CC -!- MISCELLANEOUS: There are two genes for this mannitol dehydrogenase in
CC yeast, DSF1 and YNR073C.
CC -!- SIMILARITY: Belongs to the mannitol dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; Z71688; CAA96356.1; -; Genomic_DNA.
DR EMBL; Z71689; CAA96358.1; -; Genomic_DNA.
DR EMBL; X86790; CAA60486.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10614.1; -; Genomic_DNA.
DR PIR; S50519; S50519.
DR RefSeq; NP_010844.1; NM_001178885.1.
DR RefSeq; NP_014471.3; NM_001183250.3.
DR AlphaFoldDB; P0CX09; -.
DR SMR; P0CX09; -.
DR BioGRID; 35899; 81.
DR BioGRID; 36661; 56.
DR PRIDE; P0CX09; -.
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; S000005356; MAN2.
DR VEuPathDB; FungiDB:YEL070W; -.
DR VEuPathDB; FungiDB:YNR073C; -.
DR GeneTree; ENSGT00940000176714; -.
DR HOGENOM; CLU_027324_0_1_1; -.
DR InParanoid; P0CX09; -.
DR BioCyc; YEAST:G3O-33377-MON; -.
DR PRO; PR:P0CX09; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P0CX09; protein.
DR ExpressionAtlas; P0CX09; 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 2"
FT /id="PRO_0000409748"
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
