F261_HUMAN
ID F261_HUMAN Reviewed; 471 AA.
AC P16118; B2RA88; B4DUN5; Q5JXS5; Q99951;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 {ECO:0000305};
DE Short=6PF-2-K/Fru-2,6-P2ase 1;
DE Short=PFK/FBPase 1;
DE AltName: Full=6PF-2-K/Fru-2,6-P2ase liver isozyme;
DE Includes:
DE RecName: Full=6-phosphofructo-2-kinase;
DE EC=2.7.1.105 {ECO:0000250|UniProtKB:P07953};
DE Includes:
DE RecName: Full=Fructose-2,6-bisphosphatase;
DE EC=3.1.3.46 {ECO:0000269|PubMed:2837207};
GN Name=PFKFB1 {ECO:0000312|HGNC:HGNC:8872}; Synonyms=F6PK, PFRX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=2163524; DOI=10.1093/nar/18.12.3652;
RA Lange A.J., Pilkis S.J.;
RT "Sequence of human liver 6-phosphofructo-2-kinase/fructose-2,6-
RT bisphosphatase.";
RL Nucleic Acids Res. 18:3652-3652(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Liver;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 94-471, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=2837207; DOI=10.1016/s0006-291x(88)81226-9;
RA Algaier J., Uyeda K.;
RT "Molecular cloning, sequence analysis, and expression of a human liver cDNA
RT coding for fructose-6-P,2-kinase:fructose-2,6-bisphosphatase.";
RL Biochem. Biophys. Res. Commun. 153:328-333(1988).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 40-471 IN COMPLEX WITH ATP ANALOG,
RP AND SUBUNIT.
RX PubMed=12379646; DOI=10.1074/jbc.m209105200;
RA Lee Y.H., Li Y., Uyeda K., Hasemann C.A.;
RT "Tissue-specific structure/function differentiation of the liver isoform of
RT 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.";
RL J. Biol. Chem. 278:523-530(2003).
CC -!- FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate.
CC {ECO:0000269|PubMed:2837207}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46;
CC Evidence={ECO:0000269|PubMed:2837207};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17290;
CC Evidence={ECO:0000250|UniProtKB:P07953};
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 Evidence={ECO:0000250|UniProtKB:P07953};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15654;
CC Evidence={ECO:0000250|UniProtKB:P07953};
CC -!- ACTIVITY REGULATION: Phosphorylation at Ser-33 inhibits the kinase and
CC activates the bisphosphatase. {ECO:0000250|UniProtKB:P07953}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12379646}.
CC -!- INTERACTION:
CC P16118; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-709807, EBI-742054;
CC P16118; P35557: GCK; NbExp=2; IntAct=EBI-709807, EBI-709928;
CC P16118; Q9H079: KATNBL1; NbExp=5; IntAct=EBI-709807, EBI-715394;
CC P16118; P27815-4: PDE4A; NbExp=3; IntAct=EBI-709807, EBI-12080840;
CC P16118; P16118: PFKFB1; NbExp=7; IntAct=EBI-709807, EBI-709807;
CC P16118; Q16875: PFKFB3; NbExp=3; IntAct=EBI-709807, EBI-764464;
CC P16118; Q16877: PFKFB4; NbExp=5; IntAct=EBI-709807, EBI-764534;
CC P16118; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-709807, EBI-949255;
CC P16118; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-709807, EBI-11957238;
CC P16118; Q8N554: ZNF276; NbExp=3; IntAct=EBI-709807, EBI-750821;
CC P16118; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-709807, EBI-17269964;
CC P16118; Q8N720: ZNF655; NbExp=3; IntAct=EBI-709807, EBI-625509;
CC P16118; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-709807, EBI-4395732;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P16118-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P16118-2; Sequence=VSP_054795;
CC -!- TISSUE SPECIFICITY: Liver.
CC -!- SIMILARITY: In the C-terminal section; belongs to the phosphoglycerate
CC mutase family. {ECO:0000305}.
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DR EMBL; X52638; CAA36861.1; -; mRNA.
DR EMBL; AK314089; BAG36785.1; -; mRNA.
DR EMBL; AK300724; BAG62397.1; -; mRNA.
DR EMBL; AL049732; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL020991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096079; AAH96079.1; -; mRNA.
DR EMBL; M19938; AAA35818.1; -; mRNA.
DR CCDS; CCDS14364.1; -. [P16118-1]
DR CCDS; CCDS65273.1; -. [P16118-2]
DR PIR; S12732; S12732.
DR RefSeq; NP_001258733.1; NM_001271804.1.
DR RefSeq; NP_001258734.1; NM_001271805.1. [P16118-2]
DR RefSeq; NP_002616.2; NM_002625.3. [P16118-1]
DR PDB; 1K6M; X-ray; 2.40 A; A/B=40-471.
DR PDBsum; 1K6M; -.
DR AlphaFoldDB; P16118; -.
DR BMRB; P16118; -.
DR SMR; P16118; -.
DR BioGRID; 111228; 26.
DR ComplexPortal; CPX-1992; 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 complex.
DR IntAct; P16118; 17.
DR MINT; P16118; -.
DR STRING; 9606.ENSP00000364145; -.
DR BindingDB; P16118; -.
DR ChEMBL; CHEMBL3421524; -.
DR DrugBank; DB02930; Adenosine 5'-[gamma-thio]triphosphate.
DR DrugBank; DB02393; D-Gluco-2,5-Anhydro-1-Deoxy-1-Phosphonohexitol-6-Phosphate.
DR DrugBank; DB04493; Fructose-6-phosphate.
DR DrugBank; DB04137; Guanosine-5'-Triphosphate.
DR DrugBank; DB13749; Magnesium gluconate.
DR DrugBank; DB02515; sn-glycerol 3-phosphate.
DR DEPOD; PFKFB1; -.
DR GlyGen; P16118; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P16118; -.
DR PhosphoSitePlus; P16118; -.
DR BioMuta; PFKFB1; -.
DR DMDM; 2507178; -.
DR EPD; P16118; -.
DR jPOST; P16118; -.
DR MassIVE; P16118; -.
DR PaxDb; P16118; -.
DR PeptideAtlas; P16118; -.
DR PRIDE; P16118; -.
DR ProteomicsDB; 5200; -.
DR ProteomicsDB; 53291; -. [P16118-1]
DR Antibodypedia; 533; 266 antibodies from 28 providers.
DR DNASU; 5207; -.
DR Ensembl; ENST00000375006.8; ENSP00000364145.3; ENSG00000158571.11. [P16118-1]
DR Ensembl; ENST00000545676.5; ENSP00000444074.1; ENSG00000158571.11. [P16118-2]
DR GeneID; 5207; -.
DR KEGG; hsa:5207; -.
DR MANE-Select; ENST00000375006.8; ENSP00000364145.3; NM_002625.4; NP_002616.2.
DR UCSC; uc004dty.3; human. [P16118-1]
DR CTD; 5207; -.
DR DisGeNET; 5207; -.
DR GeneCards; PFKFB1; -.
DR HGNC; HGNC:8872; PFKFB1.
DR HPA; ENSG00000158571; Group enriched (adipose tissue, liver, skeletal muscle, tongue).
DR MIM; 311790; gene.
DR neXtProt; NX_P16118; -.
DR OpenTargets; ENSG00000158571; -.
DR PharmGKB; PA33211; -.
DR VEuPathDB; HostDB:ENSG00000158571; -.
DR eggNOG; KOG0234; Eukaryota.
DR GeneTree; ENSGT00950000182835; -.
DR HOGENOM; CLU_006383_1_1_1; -.
DR InParanoid; P16118; -.
DR OMA; RHRTIYL; -.
DR OrthoDB; 392001at2759; -.
DR PhylomeDB; P16118; -.
DR TreeFam; TF313541; -.
DR BioCyc; MetaCyc:HS08310-MON; -.
DR BRENDA; 2.7.1.105; 2681.
DR BRENDA; 3.1.3.46; 2681.
DR PathwayCommons; P16118; -.
DR Reactome; R-HSA-163358; PKA-mediated phosphorylation of key metabolic factors.
DR Reactome; R-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors.
DR Reactome; R-HSA-9634600; Regulation of glycolysis by fructose 2,6-bisphosphate metabolism.
DR SABIO-RK; P16118; -.
DR SignaLink; P16118; -.
DR BioGRID-ORCS; 5207; 7 hits in 696 CRISPR screens.
DR ChiTaRS; PFKFB1; human.
DR EvolutionaryTrace; P16118; -.
DR GenomeRNAi; 5207; -.
DR Pharos; P16118; Tbio.
DR PRO; PR:P16118; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P16118; protein.
DR Bgee; ENSG00000158571; Expressed in hindlimb stylopod muscle and 105 other tissues.
DR ExpressionAtlas; P16118; baseline and differential.
DR Genevisible; P16118; HS.
DR GO; GO:0043540; C:6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004331; F:fructose-2,6-bisphosphate 2-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR GO; GO:0006094; P:gluconeogenesis; TAS:UniProtKB.
DR GO; GO:0006096; P:glycolytic process; TAS:UniProtKB.
DR GO; GO:0033133; P:positive regulation of glucokinase activity; IEA:Ensembl.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0033762; P:response to glucagon; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0042594; P:response to starvation; IEA:Ensembl.
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 InterPro; IPR001345; PG/BPGM_mutase_AS.
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.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Hydrolase;
KW Kinase; Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT CHAIN 2..471
FT /note="6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
FT 1"
FT /id="PRO_0000179960"
FT REGION 2..250
FT /note="6-phosphofructo-2-kinase"
FT REGION 251..471
FT /note="Fructose-2,6-bisphosphatase"
FT ACT_SITE 131
FT /evidence="ECO:0000255"
FT ACT_SITE 161
FT /evidence="ECO:0000255"
FT ACT_SITE 259
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT ACT_SITE 328
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 49..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12379646"
FT BINDING 82
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 105
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 133
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 139
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 170..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12379646"
FT BINDING 175
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 196
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 200
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 258
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 265
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 271
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 308
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:Q16875"
FT BINDING 339
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 350..353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 353
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 357
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 368
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 394..398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 394
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 398
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT BINDING 430
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:12379646"
FT SITE 393
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00950"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT MOD_RES 33
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07953"
FT VAR_SEQ 1..73
FT /note="MSPEMGELTQTRLQKIWIPHSSGSSRLQRRRGSSIPQFTNSPTMVIMVGLPA
FT RGKTYISTKLTRYLNWIGTPT -> MEEKTSRI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054795"
FT CONFLICT 305
FT /note="H -> R (in Ref. 1; CAA36861)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="R -> H (in Ref. 5; AAA35818)"
FT /evidence="ECO:0000305"
FT CONFLICT 397..398
FT /note="MR -> HA (in Ref. 5; AAA35818)"
FT /evidence="ECO:0000305"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 78..83
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 91..94
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 99..121
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 137..150
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:1K6M"
FT TURN 209..214
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:1K6M"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 339..345
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 347..355
FT /evidence="ECO:0007829|PDB:1K6M"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 368..384
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 394..405
FT /evidence="ECO:0007829|PDB:1K6M"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:1K6M"
FT STRAND 429..438
FT /evidence="ECO:0007829|PDB:1K6M"
FT HELIX 460..464
FT /evidence="ECO:0007829|PDB:1K6M"
SQ SEQUENCE 471 AA; 54681 MW; C4FF081A295FB7D3 CRC64;
MSPEMGELTQ TRLQKIWIPH SSGSSRLQRR RGSSIPQFTN SPTMVIMVGL PARGKTYIST
KLTRYLNWIG TPTKVFNLGQ YRREAVSYKN YEFFLPDNME ALQIRKQCAL AALKDVHNYL
SHEEGHVAVF DATNTTRERR SLILQFAKEH GYKVFFIESI CNDPGIIAEN IRQVKLGSPD
YIDCDREKVL EDFLKRIECY EVNYQPLDEE LDSHLSYIKI FDVGTRYMVN RVQDHIQSRT
VYYLMNIHVT PRSIYLCRHG ESELNIRGRI GGDSGLSVRG KQYAYALANF IQSQGISSLK
VWTSHMKRTI QTAEALGVPY EQWKALNEID AGVCEEMTYE EIQEHYPEEF ALRDQDKYRY
RYPKGESYED LVQRLEPVIM ELERQENVLV ICHQAVMRCL LAYFLDKSSD ELPYLKCPLH
TVLKLTPVAY GCKVESIYLN VEAVNTHREK PENVDITREP EEALDTVPAH Y
