6P22_YEAST
ID 6P22_YEAST Reviewed; 397 AA.
AC Q12471; D6W1T3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=6-phosphofructo-2-kinase 2;
DE Short=6PF-2-K 2;
DE EC=2.7.1.105;
DE AltName: Full=Phosphofructokinase 2 II;
GN Name=PFK27; OrderedLocusNames=YOL136C;
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=WA-1A;
RX PubMed=8861205; DOI=10.1111/j.1365-2958.1996.tb02489.x;
RA Boles E., Goehlmann H.W.H., Zimmermann F.K.;
RT "Cloning of a second gene encoding 5-phosphofructo-2-kinase in yeast, and
RT characterization of mutant strains without fructose-2,6-bisphosphate.";
RL Mol. Microbiol. 20:65-76(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896270;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1053::aid-yea993>3.0.co;2-s;
RA Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., Balcells L.,
RA Arino J., Herrero E.;
RT "Sequence analysis of a 12 801 bp fragment of the left arm of yeast
RT chromosome XV containing a putative 6-phosphofructo-2-kinase gene, a gene
RT for a possible glycophospholipid-anchored surface protein and six other
RT open reading frames.";
RL Yeast 12:1053-1058(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
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 -!- INDUCTION: By glucose and fructose, but not by galactose or maltose.
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DR EMBL; X90861; CAA62371.1; -; Genomic_DNA.
DR EMBL; Z74878; CAA99157.1; -; Genomic_DNA.
DR EMBL; X95465; CAA64733.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10649.1; -; Genomic_DNA.
DR PIR; S61066; S61066.
DR RefSeq; NP_014505.1; NM_001183390.1.
DR AlphaFoldDB; Q12471; -.
DR SMR; Q12471; -.
DR BioGRID; 34240; 77.
DR DIP; DIP-958N; -.
DR IntAct; Q12471; 1.
DR STRING; 4932.YOL136C; -.
DR iPTMnet; Q12471; -.
DR PaxDb; Q12471; -.
DR EnsemblFungi; YOL136C_mRNA; YOL136C; YOL136C.
DR GeneID; 853984; -.
DR KEGG; sce:YOL136C; -.
DR SGD; S000005496; PFK27.
DR VEuPathDB; FungiDB:YOL136C; -.
DR eggNOG; KOG0234; Eukaryota.
DR GeneTree; ENSGT00950000182835; -.
DR HOGENOM; CLU_041936_0_0_1; -.
DR InParanoid; Q12471; -.
DR OMA; QISCATI; -.
DR BioCyc; YEAST:YOL136C-MON; -.
DR Reactome; R-SCE-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
DR PRO; PR:Q12471; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12471; 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; ISA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IBA:GO_Central.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IMP:SGD.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR GO; GO:0006110; P:regulation of glycolytic process; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013079; 6Phosfructo_kin.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014379; Pfk27.
DR PANTHER; PTHR10606; PTHR10606; 1.
DR Pfam; PF01591; 6PF2K; 1.
DR PIRSF; PIRSF000711; PFK27; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Isopeptide bond; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..397
FT /note="6-phosphofructo-2-kinase 2"
FT /id="PRO_0000179977"
FT REGION 85..305
FT /note="6-phosphofructo-2-kinase"
FT ACT_SITE 197
FT /evidence="ECO:0000255"
FT ACT_SITE 235
FT /evidence="ECO:0000255"
FT BINDING 103..110
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 269
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 397 AA; 45318 MW; F8A36E8BE135A55C CRC64;
MGGSSDSDSH DGYLTSEYNS SNSLFSLNTG NSYSSASLDR ATLDCQDSVF FDNHKSSLLS
TEVPRFISND PLHLPITLNY KRDNADPTYT NGKVNKFMIV LIGLPATGKS TISSHLIQCL
KNNPLTNSLR CKVFNAGKIR RQISCATISK PLLLSNTSSE DLFNPKNNDK KETYARITLQ
KLFHEINNDE CDVGIFDATN STIERRRFIF EEVCSFNTDE LSSFNLVPII LQVSCFNRSF
IKYNIHNKSF NEDYLDKPYE LAIKDFAKRL KHYYSQFTPF SLDEFNQIHR YISQHEEIDT
SLFFFNVINA GVVEPHSLNQ SHYPSTCGKQ IRDTIMVIEN FINHYSQMFG FEYIEAVKLF
FESFGNSSEE TLTTLDSVVN DKFFDDLQSL IESNGFA
