SOL3_YEAST
ID SOL3_YEAST Reviewed; 249 AA.
AC P38858; D3DLB2;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=6-phosphogluconolactonase 3 {ECO:0000303|PubMed:15454531};
DE Short=6PGL {ECO:0000303|PubMed:15454531};
DE EC=3.1.1.31 {ECO:0000269|PubMed:15454531};
GN Name=SOL3 {ECO:0000303|PubMed:15454531}; OrderedLocusNames=YHR163W;
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 [GENOMIC DNA].
RX PubMed=8725220; DOI=10.1093/genetics/143.2.699;
RA Shen W.-C., Stanford D.R., Hopper A.K.;
RT "Los1p, involved in yeast pre-tRNA splicing, positively regulates members
RT of the SOL gene family.";
RL Genetics 143:699-712(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [3]
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 [4]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15454531; DOI=10.1534/genetics.104.030452;
RA Stanford D.R., Whitney M.L., Hurto R.L., Eisaman D.M., Shen W.-C.,
RA Hopper A.K.;
RT "Division of labor among the yeast Sol proteins implicated in tRNA nuclear
RT export and carbohydrate metabolism.";
RL Genetics 168:117-127(2004).
RN [8]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=15905473; DOI=10.1093/nar/gki583;
RA Zhang Z., Dietrich F.S.;
RT "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT SAGE.";
RL Nucleic Acids Res. 33:2838-2851(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
CC {ECO:0000269|PubMed:15454531}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate
CC + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31;
CC Evidence={ECO:0000269|PubMed:15454531};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step
CC 2/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3420 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate
CC isomerase family. 6-phosphogluconolactonase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB49323.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAB68008.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U46560; AAB49323.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00027; AAB68008.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006934; DAA06856.1; -; Genomic_DNA.
DR PIR; S48903; S48903.
DR RefSeq; NP_012033.2; NM_001179294.1.
DR AlphaFoldDB; P38858; -.
DR SMR; P38858; -.
DR BioGRID; 36597; 91.
DR DIP; DIP-5625N; -.
DR IntAct; P38858; 1.
DR STRING; 4932.YHR163W; -.
DR MaxQB; P38858; -.
DR PaxDb; P38858; -.
DR PRIDE; P38858; -.
DR EnsemblFungi; YHR163W_mRNA; YHR163W; YHR163W.
DR GeneID; 856568; -.
DR KEGG; sce:YHR163W; -.
DR SGD; S000001206; SOL3.
DR VEuPathDB; FungiDB:YHR163W; -.
DR eggNOG; KOG3147; Eukaryota.
DR GeneTree; ENSGT00550000075110; -.
DR HOGENOM; CLU_053947_0_1_1; -.
DR InParanoid; P38858; -.
DR OMA; FLVDERC; -.
DR BioCyc; YEAST:MON3O-4032; -.
DR Reactome; R-SCE-71336; Pentose phosphate pathway.
DR UniPathway; UPA00115; UER00409.
DR PRO; PR:P38858; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38858; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0017057; F:6-phosphogluconolactonase activity; IGI:SGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0009051; P:pentose-phosphate shunt, oxidative branch; IBA:GO_Central.
DR CDD; cd01400; 6PGL; 1.
DR InterPro; IPR005900; 6-phosphogluconolactonase_DevB.
DR InterPro; IPR006148; Glc/Gal-6P_isomerase.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR039104; PGLS.
DR PANTHER; PTHR11054; PTHR11054; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR01198; pgl; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..249
FT /note="6-phosphogluconolactonase 3"
FT /id="PRO_0000090084"
SQ SEQUENCE 249 AA; 27784 MW; F19B313390EA6B3D CRC64;
MVTVGVFSER ASLTHQLGEF IVKKQDEALQ KKSDFKVSVS GGSLIDALYE SLVADESLSS
RVQWSKWQIY FSDERIVPLT DADSNYGAFK RAVLDKLPST SQPNVYPMDE SLIGSDAESN
NKIAAEYERI VPQVLDLVLL GCGPDGHTCS LFPGETHRYL LNETTKRVAW CHDSPKPPSD
RITFTLPVLK DAKALCFVAE GSSKQNIMHE IFDLKNDQLP TALVNKLFGE KTSWFVNEEA
FGKVQTKTF
