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SOL4_YEAST
ID   SOL4_YEAST              Reviewed;         255 AA.
AC   P53315; D6VV28;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=6-phosphogluconolactonase 4 {ECO:0000303|PubMed:15454531};
DE            Short=6PGL {ECO:0000303|PubMed:15454531};
DE            EC=3.1.1.31 {ECO:0000269|PubMed:15454531};
GN   Name=SOL4 {ECO:0000303|PubMed:15454531}; OrderedLocusNames=YGR248W;
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].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9133742;
RX   DOI=10.1002/(sici)1097-0061(19970330)13:4<373::aid-yea82>3.0.co;2-v;
RA   Feroli F., Carignani G., Pavanello A., Guerreiro P., Azevedo D.,
RA   Rodrigues-Pousada C., Melchioretto P., Panzeri L., Agostoni Carbone M.L.;
RT   "Analysis of a 17.9 kb region from Saccharomyces cerevisiae chromosome VII
RT   reveals the presence of eight open reading frames, including BRF1
RT   (TFIIIB70) and GCN5 genes.";
RL   Yeast 13:373-377(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
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   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   [5]
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   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PATHWAY.
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).
CC   -!- FUNCTION: Involved in the pentose phosphate pathway via hydrolysis of
CC       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. {ECO:0000269|PubMed:15454531}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15454531}.
CC   -!- MISCELLANEOUS: Present with 4320 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}.
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DR   EMBL; Z73033; CAA97277.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08339.1; -; Genomic_DNA.
DR   PIR; S64574; S64574.
DR   RefSeq; NP_011764.3; NM_001181377.3.
DR   AlphaFoldDB; P53315; -.
DR   SMR; P53315; -.
DR   BioGRID; 33499; 70.
DR   IntAct; P53315; 5.
DR   MINT; P53315; -.
DR   STRING; 4932.YGR248W; -.
DR   iPTMnet; P53315; -.
DR   MaxQB; P53315; -.
DR   PaxDb; P53315; -.
DR   PRIDE; P53315; -.
DR   TopDownProteomics; P53315; -.
DR   EnsemblFungi; YGR248W_mRNA; YGR248W; YGR248W.
DR   GeneID; 853163; -.
DR   KEGG; sce:YGR248W; -.
DR   SGD; S000003480; SOL4.
DR   VEuPathDB; FungiDB:YGR248W; -.
DR   eggNOG; KOG3147; Eukaryota.
DR   GeneTree; ENSGT00550000075110; -.
DR   HOGENOM; CLU_053947_0_1_1; -.
DR   InParanoid; P53315; -.
DR   OMA; YQLFEFE; -.
DR   BioCyc; YEAST:MON3O-4047; -.
DR   UniPathway; UPA00115; UER00409.
DR   PRO; PR:P53315; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53315; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA: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; Reference proteome.
FT   CHAIN           1..255
FT                   /note="6-phosphogluconolactonase 4"
FT                   /id="PRO_0000090085"
SQ   SEQUENCE   255 AA;  28448 MW;  691C9DDA04E5BEF6 CRC64;
     MVKLQRFSEK KSLIHEFGKF ILEKQESALT GDADAVFNIA ISGGSMNQAL YESLVNDKNI
     FPHIKWPQWR IFFCDERLVP FEDPQSNYGQ FKKTVLDPLV HQGNQLNLGP TVYTINESLI
     GGGETANRKI AEEYASMLPA SFDLILLGCG EDGHTCSLFP GVEFNYLVEE MDRKVLWCNN
     SPKAPKDRIT FTLAVVAEAK SVCFLVRGAA KKAIMHDVLI VKNSELPSVL VNEMVGTKVT
     WFLDDEAGAL IPENC
 
 
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