SOU2_CANAL
ID SOU2_CANAL Reviewed; 280 AA.
AC P87218; A0A1D8PMJ6; Q5A1C2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Sorbose reductase homolog SOU2;
DE EC=1.1.-.-;
GN Name=SOU2; OrderedLocusNames=CAALFM_C406380WA;
GN ORFNames=CaO19.10415, CaO19.2897;
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).
CC -!- FUNCTION: Unknown. The enzyme has no activity toward sorbose.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
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DR EMBL; AF002134; AAC24462.1; -; Genomic_DNA.
DR EMBL; CP017626; AOW29362.1; -; Genomic_DNA.
DR RefSeq; XP_715553.2; XM_710460.2.
DR AlphaFoldDB; P87218; -.
DR SMR; P87218; -.
DR STRING; 237561.P87218; -.
DR PRIDE; P87218; -.
DR GeneID; 3642823; -.
DR KEGG; cal:CAALFM_C406380WA; -.
DR CGD; CAL0000187177; SOU2.
DR VEuPathDB; FungiDB:C4_06380W_A; -.
DR eggNOG; KOG0725; Eukaryota.
DR HOGENOM; CLU_010194_1_1_1; -.
DR InParanoid; P87218; -.
DR OMA; DGPLDHY; -.
DR OrthoDB; 1053465at2759; -.
DR PRO; PR:P87218; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IBA:GO_Central.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..280
FT /note="Sorbose reductase homolog SOU2"
FT /id="PRO_0000054778"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT BINDING 41..63
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 129..130
FT /note="EI -> KF (in Ref. 1; AAC24462)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> R (in Ref. 1; AAC24462)"
FT /evidence="ECO:0000305"
FT CONFLICT 202..203
FT /note="LS -> FT (in Ref. 1; AAC24462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 29892 MW; B96A091C75A3D297 CRC64;
MSKETTSYTN AKLGPLPTKA ATIPDNILDA FSLKGKVASV TGSSGGIGWA VAEGYAQAGA
DVAIWYNSHP ADDKAEYLTK TYGVKSKAYK CNVTDFQDVE KVVKQIESDF GTIDIFVANA
GVAWTEGPEI DVKGVDKWNK VVDVDLNSVY YCAHVVGPIF RKKGKGSFIF TASMSASIVN
VPQLQAAYNA AKAGVKHLSK SLSVEWAPFA RVNSVSPGYI ATHLSEFADP DVKSKWLQLT
PLGREAKPRE LVGAYLYLAS DAASYTTGAD LAVDGGYTVI