6P21_YEAST
ID 6P21_YEAST Reviewed; 827 AA.
AC P40433; D6VVI0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=6-phosphofructo-2-kinase 1;
DE Short=6PF-2-K 1;
DE EC=2.7.1.105;
DE AltName: Full=Phosphofructokinase 2 I;
GN Name=PFK26; OrderedLocusNames=YIL107C;
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=1657152; DOI=10.1021/bi00108a009;
RA Kretschmer M., Fraenkel D.G.;
RT "Yeast 6-phosphofructo-2-kinase: sequence and mutant.";
RL Biochemistry 30:10663-10672(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=1851090; DOI=10.1111/j.1432-1033.1991.tb15920.x;
RA Kretschmer M., Tempst P., Fraenkel D.G.;
RT "Identification and cloning of yeast phosphofructokinase 2.";
RL Eur. J. Biochem. 197:367-372(1991).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-644; SER-652 AND
RP SER-667, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Synthesis of fructose 2,6-bisphosphate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:15653, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579,
CC ChEBI:CHEBI:456216; EC=2.7.1.105;
CC -!- ACTIVITY REGULATION: Phosphorylation results in the activation of the
CC kinase activity.
CC -!- INTERACTION:
CC P40433; P11484: SSB1; NbExp=2; IntAct=EBI-1956, EBI-8627;
CC -!- MISCELLANEOUS: Present with 1710 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z38125; CAA86273.1; -; Genomic_DNA.
DR EMBL; M80801; AAA34858.1; -; Genomic_DNA.
DR EMBL; AY692819; AAT92838.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08446.1; -; Genomic_DNA.
DR PIR; S48465; S48465.
DR RefSeq; NP_012159.1; NM_001179455.1.
DR AlphaFoldDB; P40433; -.
DR SMR; P40433; -.
DR BioGRID; 34884; 187.
DR IntAct; P40433; 271.
DR MINT; P40433; -.
DR STRING; 4932.YIL107C; -.
DR iPTMnet; P40433; -.
DR MaxQB; P40433; -.
DR PaxDb; P40433; -.
DR PRIDE; P40433; -.
DR EnsemblFungi; YIL107C_mRNA; YIL107C; YIL107C.
DR GeneID; 854699; -.
DR KEGG; sce:YIL107C; -.
DR SGD; S000001369; PFK26.
DR VEuPathDB; FungiDB:YIL107C; -.
DR eggNOG; KOG0234; Eukaryota.
DR GeneTree; ENSGT00950000182835; -.
DR HOGENOM; CLU_006383_3_2_1; -.
DR InParanoid; P40433; -.
DR OMA; VISYNIQ; -.
DR BioCyc; YEAST:YIL107C-MON; -.
DR PRO; PR:P40433; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40433; protein.
DR GO; GO:0005737; C:cytoplasm; IC:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IMP:SGD.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10606; PTHR10606; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..827
FT /note="6-phosphofructo-2-kinase 1"
FT /id="PRO_0000179976"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 799..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 277
FT /evidence="ECO:0000255"
FT ACT_SITE 309
FT /evidence="ECO:0000255"
FT ACT_SITE 404
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 497
FT /evidence="ECO:0000255"
FT ACT_SITE 565
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 343
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 157
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 652
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 382
FT /note="A -> R (in Ref. 1; AAA34858)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="G -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 827 AA; 93417 MW; 9FA7BCBA08C9F0E3 CRC64;
MFKPVDFSET SPVPPDIDLA PTQSPHHVAP SQDSSYDLLS RSSDDKIDAE KGPHDELSKH
LPLFQKRPLS DTPISSNWNS PGITEENTPS DSPENSATNL KSLHRLHIND ETQLKNAKIP
TNDTTDYMPP SDGANEVTRI DLKDIKSPTR HHKRRPTTID VPGLTKSKTS PDGLISKEDS
GSKLVIVMVG LPATGKSFIT NKLSRFLNYS LYYCKVFNVG NTRRKFAKEH GLKDQDSKFF
EPKNADSTRL RDKWAMDTLD ELLDYLLEGS GSVGIFDATN TSRERRKNVL ARIRKRSPHL
KVLFLESVCS DHALVQKNIR LKLFGPDYKG KDPESSLKDF KSRLANYLKA YEPIEDDENL
QYIKMIDVGK KVIAYNIQGF LASQTVYYLL NFNLADRQIW ITRSGESEDN VSGRIGGNSH
LTPRGLRFAK SLPKFIARQR EIFYQNLMQQ KKNNENTDGN IYNDFFVWTS MRARTIGTAQ
YFNEDDYPIK QMKMLDELSA GDYDGMTYPE IKNNFPEEFE KRQKDKLRYR YPGIGGESYM
DVINRLRPVI TELERIEDNV LIITHRVVAR ALLGYFMNLS MGIIANLDVP LHCVYCLEPK
PYGITWSLWE YDEASDSFSK VPQTDLNTTR VKEVGLVYNE RRYSVIPTAP PSARSSFASD
FLSRKRSNPT SASSSQSELS EQPKNSVSAQ TGSNNTTLIG SNFNIKNENG DSRIPLSAPL
MATNTSNNIL DGGGTSISIH RPRVVPNQNN VNPLLANNNK AASNVPNVKK SAATPRQIFE
IDKVDEKLSM LKNKSFLLHG KDYPNNADNN DNEDIRAKTM NRSQSHV
