ID A4QNV1_DANRE Unreviewed; 776 AA. AC A4QNV1; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03184}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03184}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03184}; GN Name=pfkmb {ECO:0000313|EMBL:AAI39533.1, GN ECO:0000313|ZFIN:ZDB-GENE-081114-1}; GN Synonyms=im:7137110 {ECO:0000313|RefSeq:NP_001082886.1}, wu:fc58g11 GN {ECO:0000313|RefSeq:NP_001082886.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI39533.1}; RN [1] {ECO:0000313|RefSeq:NP_001082886.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12477932; DOI=10.1073/pnas.242603899; RG Mammalian Gene Collection Program Team; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., Klausner R.D., RA Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., Altschul S.F., RA Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., Hopkins R.F., Jordan H., RA Moore T., Max S.I., Wang J., Hsieh F., Diatchenko L., Marusina K., RA Farmer A.A., Rubin G.M., Hong L., Stapleton M., Soares M.B., Bonaldo M.F., RA Casavant T.L., Scheetz T.E., Brownstein M.J., Usdin T.B., Toshiyuki S., RA Carninci P., Prange C., Raha S.S., Loquellano N.A., Peters G.J., RA Abramson R.D., Mullahy S.J., Bosak S.A., McEwan P.J., McKernan K.J., RA Malek J.A., Gunaratne P.H., Richards S., Worley K.C., Hale S., Garcia A.M., RA Gay L.J., Hulyk S.W., Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., Rodriguez A.C., RA Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Krzywinski M.I., RA Skalska U., Smailus D.E., Schnerch A., Schein J.E., Jones S.J., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human and RT mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [2] {ECO:0000313|EMBL:AAI39533.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Whole body {ECO:0000313|EMBL:AAI39533.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [4] {ECO:0000313|RefSeq:NP_001082886.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (NOV-2023) to UniProtKB. 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:0000256|HAMAP-Rule:MF_03184}. 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; CC Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP- CC Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP- CC Rule:MF_03184}; CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate. CC {ECO:0000256|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:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_03184, CC ECO:0000256|PIRNR:PIRNR000533}. CC -!- SUBUNIT: Homo- and heterotetramers. {ECO:0000256|HAMAP-Rule:MF_03184}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184}. 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:0000256|PIRNR:PIRNR000533}. 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:0000256|HAMAP-Rule:MF_03184}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03184}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC139532; AAI39533.1; -; mRNA. DR RefSeq; NP_001082886.1; NM_001089417.1. DR GeneID; 568001; -. DR KEGG; dre:568001; -. DR AGR; ZFIN:ZDB-GENE-081114-1; -. DR CTD; 568001; -. DR ZFIN; ZDB-GENE-081114-1; pfkmb. DR OrthoDB; 374214at2759; -. DR PhylomeDB; A4QNV1; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000000437; Alternate scaffold 6. DR Proteomes; UP000000437; Chromosome 6. DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central. DR GO; GO:0016208; F:AMP binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central. DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. 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:SF56; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 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. PE 1: Evidence at protein level; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03184}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03184}; KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP- KW Rule:MF_03184}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03184}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03184}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_03184}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A4QNV1}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_03184}. FT DOMAIN 18..323 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT DOMAIN 401..685 FT /note="Phosphofructokinase" FT /evidence="ECO:0000259|Pfam:PF00365" FT REGION 1..390 FT /note="N-terminal catalytic PFK domain 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 401..776 FT /note="C-terminal regulatory PFK domain 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT ACT_SITE 166 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 25 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 88..89 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 118..121 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_03184" FT BINDING 201 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_03184" FT BINDING 292 FT /ligand="substrate" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_03184" FT BINDING 470 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:0000256|HAMAP-Rule:MF_03184" FT BINDING 527..531 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:0000256|HAMAP-Rule:MF_03184" FT BINDING 565 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:0000256|HAMAP-Rule:MF_03184" FT BINDING 572..574 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:0000256|HAMAP-Rule:MF_03184" FT BINDING 628 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:0000256|HAMAP-Rule:MF_03184" FT BINDING 654 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:0000256|HAMAP-Rule:MF_03184" FT BINDING 660..663 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:0000256|HAMAP-Rule:MF_03184" FT BINDING 734 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:0000256|HAMAP-Rule:MF_03184" SQ SEQUENCE 776 AA; 84166 MW; 92D93282047C995D CRC64; MQHSAPVDPT KMGVGRAIAV LTSGGDAQGM NAAVRATVRV GIYTGAKVYF VHEGYQGLVD GGDNIRQATW ESVSMMLQLG GTVIGSARCQ DFRTKEGRAK AACNLVKLGI TNLCVIGGDG SLTGANEFRN EWSELLQILQ KAGKITAEEA KCSSHLNIVG MVGSIDNDFC GTDMTIGTDS ALHRIMEVVD AITTTAQSHQ RAFILEVMGR HCGYLALVTA LSCGADWVFI PEMPPDEGWE DHLCRRLTYQ RSIGNRLNVI IVAEGALDRH GKPITCDIIK NLVTKKLGFD TRATILGHVQ RGGTPSAFDR ILGSRMGVEA VMALLEATPD TPACVVSLSG NMAVRLPLME CVQVTKEVTK AMAEGRFEEA IKLRGKSFEN NWNTYKLLAH VTAPDVKSNI NIAILNVGAP CAGMNAAVRS AVRIGILQGH NMLAVHDGFE GLANGTIEPM AWGYVGGWTG KGGSILGTKR SLPANMIEEI SLNIAKFNIH ALVIIGGFEA FVGGLELVTA REKYEELCIP LVVIPATVSN NVPGSDFSVG ADTALNTITT TCDRIKQSAA GTKRRVFIIE TMGGYCGYLA TMAGLAAGAD AAYVFEDPFG IHDLEANVEH LLEKMKTTVK RGLILRNEKC NANYTTDFLF NLYSEEGKGV FDCRKNVLGH MQQGGTPTPF DRNFGTKMGA KAVLWLTDKL KECYRHGRIF ANTPDSACVL GMRKRAMLFQ PLSDLKEDTD FEHRIPKTEW WLKLRPILKI LAKYKISLDT SETATMEHVI KKRGGV //