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   27-MAR-2024, entry version 206.
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,
RC   Pancreas, 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; 33.
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; 7.
DR   MINT; P47857; -.
DR   STRING; 10090.ENSMUSP00000059801; -.
DR   GlyCosmos; P47857; 1 site, No reported glycans.
DR   GlyGen; P47857; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; P47857; -.
DR   MetOSite; P47857; -.
DR   PhosphoSitePlus; P47857; -.
DR   SwissPalm; P47857; -.
DR   EPD; P47857; -.
DR   jPOST; P47857; -.
DR   MaxQB; P47857; -.
DR   PaxDb; 10090-ENSMUSP00000059801; -.
DR   PeptideAtlas; P47857; -.
DR   ProteomicsDB; 288100; -. [P47857-1]
DR   ProteomicsDB; 288101; -. [P47857-2]
DR   ProteomicsDB; 288102; -. [P47857-3]
DR   Pumba; P47857; -.
DR   Antibodypedia; 1061; 520 antibodies from 37 providers.
DR   DNASU; 18642; -.
DR   Ensembl; ENSMUST00000051226.8; ENSMUSP00000059801.7; ENSMUSG00000033065.15. [P47857-1]
DR   Ensembl; ENSMUST00000163507.8; ENSMUSP00000132803.2; ENSMUSG00000033065.15. [P47857-1]
DR   Ensembl; ENSMUST00000230445.2; ENSMUSP00000155809.2; ENSMUSG00000033065.15. [P47857-1]
DR   GeneID; 18642; -.
DR   KEGG; mmu:18642; -.
DR   UCSC; uc007xlv.2; mouse. [P47857-1]
DR   AGR; MGI:97548; -.
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; WHNLGGS; -.
DR   OrthoDB; 374214at2759; -.
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 77 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 263 other cell types or tissues.
DR   ExpressionAtlas; P47857; baseline and differential.
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: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; 3.40.50.450; -; 2.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 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   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF59; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, MUSCLE TYPE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
DR   Genevisible; P47857; MM.
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
//