ID   YL345_YEAST             Reviewed;         509 AA.
AC   Q06137;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Putative 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase YLR345W;
DE   Includes:
DE     RecName: Full=6-phosphofructo-2-kinase;
DE              EC=2.7.1.105;
DE   Includes:
DE     RecName: Full=Fructose-2,6-bisphosphatase;
DE              EC=3.1.3.46;
GN   OrderedLocusNames=YLR345W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313267; PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
RA   Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
RA   Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
RA   Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
RA   Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
RA   Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
RA   Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
RA   Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
RA   Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
RA   Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
RA   Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
RA   Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923954; 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   [3]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [4]
RP   INDUCTION.
RX   PubMed=15494396; DOI=10.1074/jbc.M404669200;
RA   Zaim J., Speina E., Kierzek A.M.;
RT   "Identification of new genes regulated by the Crt1 transcription
RT   factor, an effector of the DNA damage checkpoint pathway in
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 280:28-37(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, AND MASS
RP   SPECTROMETRY.
RX   PubMed=17563356; DOI=10.1073/pnas.0701622104;
RA   Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
RT   "Proteome-wide identification of in vivo targets of DNA damage
RT   checkpoint kinases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-75 AND SER-432,
RP   AND MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Beta-D-fructose 2,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + beta-D-
CC       fructose 2,6-bisphosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- INTERACTION:
CC       Q06146:-; NbExp=1; IntAct=EBI-33827, EBI-36149;
CC       P48240:MTR3; NbExp=1; IntAct=EBI-33827, EBI-1749;
CC       P09938:RNR2; NbExp=1; IntAct=EBI-33827, EBI-15240;
CC       Q06168:SFH1; NbExp=1; IntAct=EBI-33827, EBI-35813;
CC       P38634:SIC1; NbExp=1; IntAct=EBI-33827, EBI-17127;
CC       P38426:TPS3; NbExp=1; IntAct=EBI-33827, EBI-19448;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Expression is under the control of the RFX1
CC       transcription factor.
CC   -!- MISCELLANEOUS: Present with 3380 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       phosphoglycerate mutase family.
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DR   EMBL; U19028; AAB67253.1; -; Genomic_DNA.
DR   PIR; S51348; S51348.
DR   RefSeq; NP_013449.1; -.
DR   HSSP; P25114; 1BIF.
DR   DIP; DIP:1500N; -.
DR   IntAct; Q06137; 18.
DR   PeptideAtlas; Q06137; -.
DR   Ensembl; YLR345W; Saccharomyces cerevisiae.
DR   GeneID; 851059; -.
DR   GenomeReviews; Y13138_GR; YLR345W.
DR   KEGG; sce:YLR345W; -.
DR   NMPDR; fig|4932.3.peg.4470; -.
DR   CYGD; YLR345w; -.
DR   SGD; S000004337; YLR345W.
DR   HOGENOM; Q06137; -.
DR   OMA; Q06137; SYHDLAV.
DR   BRENDA; 2.7.1.105; 250.
DR   BRENDA; 3.1.3.46; 250.
DR   NextBio; 967684; -.
DR   GermOnline; YLR345W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; NAS:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase act...; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; NAS:SGD.
DR   GO; GO:0006110; P:regulation of glycolysis; NAS:SGD.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
DR   InterPro; IPR013078; PG_mutase.
DR   PANTHER; PTHR10606; 6Pfruct_kin; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Cytoplasm; Hydrolase; Kinase;
KW   Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW   Transferase.
FT   CHAIN         1    509       Putative 6-phosphofructo-2-
FT                                kinase/fructose-2,6-biphosphatase
FT                                YLR345W.
FT                                /FTId=PRO_0000268185.
FT   NP_BIND      90     97       ATP (By similarity).
FT   REGION        6    291       6-phosphofructo-2-kinase (By similarity).
FT   REGION      292    466       Fructose-2,6-bisphosphatase (By
FT                                similarity).
FT   ACT_SITE    173    173       Potential.
FT   ACT_SITE    459    459       Proton donor (By similarity).
FT   BINDING     237    237       Fructose-6-phosphate (By similarity).
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES      75     75       Phosphoserine.
FT   MOD_RES     104    104       Phosphothreonine.
FT   MOD_RES     432    432       Phosphoserine.
SQ   SEQUENCE   509 AA;  58386 MW;  29718CA8ECA8EB4E CRC64;
     MPNVLSDDEE LLNGLGSEIM KPSRQGNHMA RTVKRWVNKE RATTADLKNV NIDGVHGPVN
     TESYISPGQL YSTDSGNLFH AGRILVVLVG LPATSKTLLS VAITRYTRWL GVRTKSFHFS
     EYKESAKNIP SDYFCVVPTS KEGVAFVEKL RMQMLNDILA FFNDLSGQLA IYDALNIRKI
     DRKNLETTFS EIGVKVLFIE SIVSDQEIMN RNIALALESN DYKGLSTDEA IDEYMRRLSV
     NEPYYEMMTH DEELSYIKYI NLGKQIIVKD NIHGYLVNKI VFFLMNLRQK KGCVYFARCG
     TSDKDNYIHD EELNEEGIHY SQVLKDFVLQ RIKQKRQAKK NSDSLVEVID GSHDEDLKTS
     LIVWTGPRKR THDTALFFSK EGIKVQQRSE LRQLNPGSIA DLTDQQIMDK FPSEYKESLK
     DPYHFRFPRA ESYHDLAVRM EPLLLEMEHT SKDILIIAHE STLRVLYGYL MACTCVELPN
     LNFTRDKLVE ISFSPFCNTV ELLNIPLTS
//