PFKAM_MOUSE
ID PFKAM_MOUSE Reviewed; 780 AA.
AC P47857; C8CMN5; C8CMN6; C8CMN7; O35513; Q543L1; Q9JK94;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=ATP-dependent 6-phosphofructokinase, muscle type {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=PFK-M;
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=6-phosphofructokinase type A;
DE AltName: Full=Phosphofructo-1-kinase isozyme A;
DE Short=PFK-A;
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=Pfkm; Synonyms=Pfk-m, Pfka;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=SWR/J; TISSUE=Brain;
RX PubMed=11137296; DOI=10.1016/s0378-1119(00)00463-7;
RA Gunasekera D., Kemp R.G.;
RT "Genomic organization, 5'flanking region and tissue-specific expression of
RT mouse phosphofructokinase C gene.";
RL Gene 260:103-112(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Kidney, Spinal cord, and Thymus {ECO:0000312|EMBL:AK138788};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-213 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 259-345.
RC STRAIN=ICR;
RX PubMed=7980403; DOI=10.1042/bj3030449;
RA Nakajima H., Noguchi T., Hamaguchi T., Tomita K., Hanafusa T., Kono N.,
RA Tanaka T., Kuwajima M., Matsuzawa Y.;
RT "Expression of mouse phosphofructokinase-M gene alternative transcripts:
RT evidence for the conserved two-promoter system.";
RL Biochem. J. 303:449-453(1994).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, CATALYTIC
RP ACTIVITY, INTERACTION WITH GSTM5 AND HK1, SUBCELLULAR LOCATION, ALTERNATIVE
RP SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:ACU65459.1};
RX PubMed=19889946; DOI=10.1095/biolreprod.109.080580;
RA Nakamura N., Mori C., Eddy E.M.;
RT "Molecular complex of three testis-specific isozymes associated with the
RT mouse sperm fibrous sheath: hexokinase 1, phosphofructokinase M, and
RT glutathione S-transferase mu class 5.";
RL Biol. Reprod. 82:504-515(2010).
RN [5]
RP PROTEIN SEQUENCE OF 367-374, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184,
CC ECO:0000269|PubMed:19889946}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03184, ECO:0000269|PubMed:19889946};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBUNIT: Homo- and heterotetramers (By similarity). Phosphofructokinase
CC (PFK) enzyme functions as a tetramer composed of different combinations
CC of 3 types of subunits, called PFKM (M), PFKL (L) and PFKP (P). The
CC composition of the PFK tetramer differs according to the tissue type it
CC is present in. The kinetic and regulatory properties of the tetrameric
CC enzyme are dependent on the subunit composition, hence can vary across
CC tissues (Probable). Isoform 2 and isoform 3 interact (via N-terminal
CC testis-specific region) with GSTM5. Isoform 2 and isoform 3 interact
CC (via C-terminus) with HK1 (via N-terminal spermatogenic cell-specific
CC region). {ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:19889946,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:19889946}. Note=Principal piece region of the sperm
CC flagellum. {ECO:0000269|PubMed:19889946}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:19889946}. Note=Principal piece region of the sperm
CC flagellum. {ECO:0000269|PubMed:19889946}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P47857-1; Sequence=Displayed;
CC Name=2; Synonyms=Pfkms_V4 {ECO:0000303|PubMed:19889946};
CC IsoId=P47857-2; Sequence=VSP_057079;
CC Name=3; Synonyms=Pfkms_V3 {ECO:0000303|PubMed:19889946};
CC IsoId=P47857-3; Sequence=VSP_057080;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in skeletal muscle (at
CC protein level). Isoform 2 and isoform 3 are testis-specific and are
CC detected in quiescent sperm (at protein level). They are first detected
CC in the cytoplasm of round spermatids and subsequently in the flagellum
CC of elongated spermatids extending into the seminiferous tubule lumen
CC (at protein level). Isoform 2 is expressed at higher level than isoform
CC 3 in testis. {ECO:0000269|PubMed:19889946}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 and isoform 3 are first seen on
CC postnatal day 16 corresponding to the age when midpachytene
CC spermatocytes are present in the synchronous first wave of
CC spermatogenesis. Isoform 2 and isoform 3 levels increase substantially
CC between days 14 and 18 and continue to increase to age 30 days of
CC neonatal testis development. {ECO:0000269|PubMed:19889946}.
CC -!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK138788; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305|PubMed:19889946};
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DR EMBL; AF249894; AAF63762.1; -; mRNA.
DR EMBL; AK002711; BAB22303.1; -; mRNA.
DR EMBL; AK049773; BAC33913.1; -; mRNA.
DR EMBL; AK138788; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; D21864; BAA21892.1; -; Genomic_DNA.
DR EMBL; D21865; BAA21012.1; -; mRNA.
DR EMBL; GQ428204; ACU65458.1; -; mRNA.
DR EMBL; GQ428205; ACU65459.1; -; mRNA.
DR EMBL; GQ428206; ACU65460.1; -; mRNA.
DR CCDS; CCDS27786.1; -. [P47857-1]
DR PIR; S53317; S53317.
DR RefSeq; NP_001156959.1; NM_001163487.1. [P47857-1]
DR RefSeq; NP_001156960.1; NM_001163488.1. [P47857-1]
DR RefSeq; NP_067489.3; NM_021514.4. [P47857-1]
DR RefSeq; XP_006520664.1; XM_006520601.3. [P47857-2]
DR RefSeq; XP_006520665.1; XM_006520602.2.
DR AlphaFoldDB; P47857; -.
DR SMR; P47857; -.
DR BioGRID; 202125; 31.
DR ComplexPortal; CPX-2049; 6-phosphofructokinase, M4 homotetramer.
DR ComplexPortal; CPX-2055; 6-phosphofructokinase, ML3 heterotetramer.
DR ComplexPortal; CPX-2056; 6-phosphofructokinase, M2L2 heterotetramer.
DR ComplexPortal; CPX-2057; 6-phosphofructokinase, M3L heterotetramer.
DR IntAct; P47857; 6.
DR MINT; P47857; -.
DR STRING; 10090.ENSMUSP00000059801; -.
DR GlyGen; P47857; 1 site.
DR iPTMnet; P47857; -.
DR PhosphoSitePlus; P47857; -.
DR SwissPalm; P47857; -.
DR EPD; P47857; -.
DR jPOST; P47857; -.
DR MaxQB; P47857; -.
DR PaxDb; P47857; -.
DR PeptideAtlas; P47857; -.
DR PRIDE; P47857; -.
DR ProteomicsDB; 288100; -. [P47857-1]
DR ProteomicsDB; 288101; -. [P47857-2]
DR ProteomicsDB; 288102; -. [P47857-3]
DR Antibodypedia; 1061; 478 antibodies from 37 providers.
DR DNASU; 18642; -.
DR Ensembl; ENSMUST00000051226; ENSMUSP00000059801; ENSMUSG00000033065. [P47857-1]
DR Ensembl; ENSMUST00000163507; ENSMUSP00000132803; ENSMUSG00000033065. [P47857-1]
DR Ensembl; ENSMUST00000230445; ENSMUSP00000155809; ENSMUSG00000033065. [P47857-1]
DR GeneID; 18642; -.
DR KEGG; mmu:18642; -.
DR UCSC; uc007xlv.2; mouse. [P47857-1]
DR CTD; 5213; -.
DR MGI; MGI:97548; Pfkm.
DR VEuPathDB; HostDB:ENSMUSG00000033065; -.
DR eggNOG; KOG2440; Eukaryota.
DR GeneTree; ENSGT00940000155440; -.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; P47857; -.
DR OMA; SRYAVKC; -.
DR OrthoDB; 172878at2759; -.
DR PhylomeDB; P47857; -.
DR TreeFam; TF300411; -.
DR Reactome; R-MMU-70171; Glycolysis.
DR SABIO-RK; P47857; -.
DR UniPathway; UPA00109; UER00182.
DR BioGRID-ORCS; 18642; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Pfkm; mouse.
DR PRO; PR:P47857; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P47857; protein.
DR Bgee; ENSMUSG00000033065; Expressed in triceps brachii and 260 other tissues.
DR ExpressionAtlas; P47857; baseline and differential.
DR Genevisible; P47857; MM.
DR GO; GO:0005945; C:6-phosphofructokinase complex; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0097228; C:sperm principal piece; IDA:MGI.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IDA:MGI.
DR GO; GO:0016208; F:AMP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
DR GO; GO:0070061; F:fructose binding; ISO:MGI.
DR GO; GO:0070095; F:fructose-6-phosphate binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0008443; F:phosphofructokinase activity; IDA:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0061621; P:canonical glycolysis; IDA:MGI.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISO:MGI.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; ISO:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0005980; P:glycogen catabolic process; IMP:MGI.
DR GO; GO:0093001; P:glycolysis from storage polysaccharide through glucose-1-phosphate; IMP:MGI.
DR GO; GO:0006096; P:glycolytic process; ISO:MGI.
DR GO; GO:0061615; P:glycolytic process through fructose-6-phosphate; IDA:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR CDD; cd00764; Eukaryotic_PFK; 1.
DR Gene3D; 3.40.50.460; -; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR041914; PFK_vert-type.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Cell projection; Cilium; Cytoplasm; Direct protein sequencing; Flagellum;
KW Glycolysis; Glycoprotein; Hydroxylation; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P00511"
FT CHAIN 2..780
FT /note="ATP-dependent 6-phosphofructokinase, muscle type"
FT /id="PRO_0000112018"
FT REGION 2..390
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 391..401
FT /note="Interdomain linker"
FT REGION 402..780
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 88..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 118..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 164..166
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 201
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 208..210
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 264
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 292
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 298..301
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 471
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 528..532
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 566
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 573..575
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 629
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 655
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 661..664
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 735
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_note="allosteric activator; ligand shared between
FT dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:P00511"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47858"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 557
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000250|UniProtKB:P08237"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08237"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00511"
FT CARBOHYD 530
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MRREEFQLRFFMCVIESRQVVRTTQSTAGEASTSNMTIPESKADDQW
FT RLDGMDDDPSTVGPVSIPDTEWIM (in isoform 2)"
FT /evidence="ECO:0000269|PubMed:19889946"
FT /id="VSP_057079"
FT VAR_SEQ 1
FT /note="M -> MEEKLTCSFKLLTELLNLITPLAQALFGKRLQNSILDPGDCLSEFTL
FT EERKASGICQPHLFSKHKEINLFLQGILTCYEVAMRREEFQLRFFMCVIESRQVVRTTQ
FT STAGEASTSNMTIPESKADDQWRLDGMDDDPSTVGPVSIPDTEWIM (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:19889946"
FT /id="VSP_057080"
SQ SEQUENCE 780 AA; 85269 MW; 7917C7AC108B25C7 CRC64;
MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD
GGEHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG
SLTGADTFRS EWSDLLNDLQ KDGKITAEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS
ALHRIVEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE
EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK
AMDEKRFDEA IKLRGRSFMN NWEVYKLLAH VRPPVSKGGL HTVAVMNVGA PAAGMNAAVR
STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKNLEQ
ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSI
GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG
HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF
QPVTELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI SRKRSGEAAV
