SOU1_CANAL
ID SOU1_CANAL Reviewed; 281 AA.
AC P87219; A0A1D8PMK2; Q5A1C3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Sorbose reductase SOU1;
DE EC=1.1.1.289 {ECO:0000269|PubMed:16134116};
DE AltName: Full=Sorbitol utilization protein SOU1;
GN Name=SOU1; OrderedLocusNames=CAALFM_C406390WA;
GN ORFNames=CaO19.10414, CaO19.2896;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SOR17;
RX PubMed=9560244; DOI=10.1073/pnas.95.9.5150;
RA Janbon G., Sherman F., Rustchenko E.;
RT "Monosomy of a specific chromosome determines L-sorbose utilization: a
RT novel regulatory mechanism in Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:5150-5155(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=16134116; DOI=10.1002/yea.1282;
RA Greenberg J.R., Price N.P., Oliver R.P., Sherman F., Rustchenko E.;
RT "Candida albicans SOU1 encodes a sorbose reductase required for L-sorbose
RT utilization.";
RL Yeast 22:957-969(2005).
CC -!- FUNCTION: Catalyzes the NADP dependent reduction of L-sorbose to D-
CC glucitol. Can also convert fructose to mannitol, but less efficiently.
CC {ECO:0000269|PubMed:16134116}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-sorbitol + NADP(+) = H(+) + keto-L-sorbose + NADPH;
CC Xref=Rhea:RHEA:14609, ChEBI:CHEBI:13172, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17924, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.289; Evidence={ECO:0000269|PubMed:16134116};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.95 uM for sorbose {ECO:0000269|PubMed:16134116};
CC Vmax=378 umol/min/mg enzyme with sorbose as substrate
CC {ECO:0000269|PubMed:16134116};
CC Vmax=74 umol/min/mg enzyme with fructose as substrate
CC {ECO:0000269|PubMed:16134116};
CC pH dependence:
CC Optimum pH is 6.2. {ECO:0000269|PubMed:16134116};
CC -!- PATHWAY: Carbohydrate degradation; L-sorbose degradation.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16134116}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF002134; AAC24463.1; -; Genomic_DNA.
DR EMBL; CP017626; AOW29363.1; -; Genomic_DNA.
DR RefSeq; XP_715552.1; XM_710459.2.
DR AlphaFoldDB; P87219; -.
DR SMR; P87219; -.
DR STRING; 237561.P87219; -.
DR GeneID; 3642799; -.
DR KEGG; cal:CAALFM_C406390WA; -.
DR CGD; CAL0000190633; SOU1.
DR VEuPathDB; FungiDB:C4_06390W_A; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; P87219; -.
DR OMA; HGGGEYP; -.
DR OrthoDB; 1053465at2759; -.
DR BRENDA; 1.1.1.289; 1096.
DR BRENDA; 1.1.1.B3; 1096.
DR UniPathway; UPA00103; -.
DR PRO; PR:P87219; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0050085; F:mannitol 2-dehydrogenase (NADP+) activity; IDA:CGD.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IBA:GO_Central.
DR GO; GO:0032115; F:sorbose reductase activity; IDA:CGD.
DR GO; GO:0042850; P:L-sorbose catabolic process; IDA:CGD.
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 Carbohydrate metabolism; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..281
FT /note="Sorbose reductase SOU1"
FT /id="PRO_0000054776"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 281 AA; 30038 MW; 8D5A1F54B7259F19 CRC64;
MSEEIISFTN PALGPLPTKA PQLPSNVLDL FSLKGKVASV TGSSGGIGWA VAEAFAQAGA
DVAIWYNSKP ADAKAEYLTE KYGVKAKAYK CNVTDPNDVS KVINEIEKDF GTIDIFVANA
GVAWTDGPEI DVQGYDQWKK IVDCDLNGVY YCAHTVGQIF KKNKSGSLII TSSMSGTIVN
IPQLQAPYNA AKAACTHLAK SLSVEWASFG ARVNSISPGY ILTDIADFAD PEMKKKWWQL
TPLGREGLPQ ELVGAYLYLA SNASTYTTGS NIAVDGGYTC P
