SDR_YARLI
ID SDR_YARLI Reviewed; 278 AA.
AC Q6CEE9;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable NADP-dependent mannitol dehydrogenase;
DE Short=MtDH;
DE EC=1.1.1.138 {ECO:0000269|PubMed:23608762};
DE AltName: Full=Mannitol 2-dehydrogenase [NADP(+)];
DE AltName: Full=Short chain dehydrogenase/reductase;
DE Short=YlSDR;
GN OrderedLocusNames=YALI0B16192g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [2]
RP FUNCTION.
RC STRAIN=CLIB 122 / E 150;
RX DOI=10.3390/biom3030449;
RA Napora-Wijata K., Strohmeier G.A., Sonavane M.N., Avi M., Robins K.,
RA Winkler M.;
RT "Enantiocomplementary Yarrowia lipolytica oxidoreductases: Alcohol
RT dehydrogenase 2 and short chain dehydrogenase/reductase.";
RL Biomolecules 3:449-460(2013).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=CLIB 122 / E 150;
RX PubMed=23608762; DOI=10.1016/j.bmcl.2013.03.064;
RA Napora K., Wrodnigg T.M., Kosmus P., Thonhofer M., Robins K., Winkler M.;
RT "Yarrowia lipolytica dehydrogenase/reductase: an enzyme tolerant for
RT lipophilic compounds and carbohydrate substrates.";
RL Bioorg. Med. Chem. Lett. 23:3393-3395(2013).
CC -!- FUNCTION: Versatile oxidoreductase that catalyzes the oxidation and
CC reduction of polar as well as non-polar substrates at a very broad pH
CC range. Preferentially oxidizes secondary alcohols. Has highest activity
CC for racemic 2-heptanol and racemic octanol. Is also an efficient
CC reductase for selected substrates. Substrate selectivity was found for
CC medium chain length ketones with the carbonyl function at position C-2.
CC Has highest activities for ribulose and fructose. The enzyme is (R)-
CC selective in the reduction direction and produces exclusively the (R)-
CC enantiomer. {ECO:0000269|PubMed:23608762, ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol + NADP(+) = D-fructose + H(+) + NADPH;
CC Xref=Rhea:RHEA:16765, ChEBI:CHEBI:15378, ChEBI:CHEBI:16899,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.138; Evidence={ECO:0000269|PubMed:23608762};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.91 mM for rac-2-heptanol {ECO:0000269|PubMed:23608762};
CC KM=8.8 mM for ribulose {ECO:0000269|PubMed:23608762};
CC KM=0.793 mM for NADP(+) {ECO:0000269|PubMed:23608762};
CC Note=kcat is 3.17 sec(-1) with rac-2-heptanol as substrate and 6.15
CC sec(-1) for NADP(+). kcat is 5.42 sec(-1) for ribulose.;
CC pH dependence:
CC Optimum pH is 10 for the oxidation reaction, and 4-9 for the
CC reduction reaction. {ECO:0000269|PubMed:23608762};
CC Temperature dependence:
CC Optimum temperature is 25-28 degrees Celsius.
CC {ECO:0000269|PubMed:23608762};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O93868}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; CR382128; CAG83216.1; -; Genomic_DNA.
DR RefSeq; XP_500963.1; XM_500963.1.
DR AlphaFoldDB; Q6CEE9; -.
DR SMR; Q6CEE9; -.
DR STRING; 4952.CAG83216; -.
DR EnsemblFungi; CAG83216; CAG83216; YALI0_B16192g.
DR GeneID; 2906628; -.
DR KEGG; yli:YALI0B16192g; -.
DR VEuPathDB; FungiDB:YALI0_B16192g; -.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; Q6CEE9; -.
DR OMA; AVEWVGF; -.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0050085; F:mannitol 2-dehydrogenase (NADP+) activity; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; ISS:UniProtKB.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IBA:GO_Central.
DR GO; GO:0019594; P:mannitol metabolic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..278
FT /note="Probable NADP-dependent mannitol dehydrogenase"
FT /id="PRO_0000425282"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT ACT_SITE 190
FT /note="Lowers pKa of active site Tyr"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 117
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 186
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
FT BINDING 218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:O93868"
SQ SEQUENCE 278 AA; 30033 MW; EA8D8F12F578FFEC CRC64;
MPAPATYATG LTPLPTPVPK VSKNIMERFS LKGKVASITG SSSGIGFAVA EAFAQAGADV
AIWYNSKPSD EKAEYLSKTY GVRSKAYKCA VTNAKQVETT IQTIEKDFGK IDIFIANAGI
PWTAGPMIDV PNNEEWDKVV DLDLNGAYYC AKYAGQIFKK QGYGSFIFTA SMSGHIVNIP
QMQACYNAAK CAVLHLSRSL AVEWAGFARC NTVSPGYMAT EISDFIPRDT KEKWWQLIPM
GREGDPSELA GAYIYLASDA STYTTGADIL VDGGYCCP
