ID A0A1J9P7U8_9EURO Unreviewed; 805 AA. AC A0A1J9P7U8; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 11-DEC-2019, entry version 16. 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 ORFNames=AJ78_07186 {ECO:0000313|EMBL:OJD12174.1}; OS Emergomyces pasteurianus Ep9510. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces. OX NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD12174.1, ECO:0000313|Proteomes:UP000182235}; RN [1] {ECO:0000313|EMBL:OJD12174.1, ECO:0000313|Proteomes:UP000182235} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD12174.1, RC ECO:0000313|Proteomes:UP000182235}; RG The Broad Institute Genomics Platform; RA Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K., RA McEwen J.G.; RT "Emmonsia species relationships and genome sequence."; RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases. 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; Evidence={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|HAMAP-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|HAMAP-Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533}. CC -!- SUBUNIT: Homotetramer. {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: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OJD12174.1}. 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; LGRN01000437; OJD12174.1; -; Genomic_DNA. DR OrthoDB; 172878at2759; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000182235; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro. DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1. DR InterPro; IPR009161; 6-Pfructokinase_euk. DR InterPro; IPR022953; ATP_PFK. 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 3: Inferred from homology; 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|HAMAP-Rule:MF_03184}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533, KW ECO:0000313|EMBL:OJD12174.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_03184}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03184}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}; KW Reference proteome {ECO:0000313|Proteomes:UP000182235}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_03184, KW ECO:0000256|PIRNR:PIRNR000533}. FT DOMAIN 17..324 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT DOMAIN 406..701 FT /note="PFK" FT /evidence="ECO:0000259|Pfam:PF00365" FT NP_BIND 88..89 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT NP_BIND 118..121 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 1..391 FT /note="N-terminal catalytic PFK domain 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 164..166 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 208..210 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 299..302 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 392..405 FT /note="Interdomain linker" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 406..805 FT /note="C-terminal regulatory PFK domain 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 539..543 FT /note="Allosteric activator fructose 2,6-bisphosphate FT binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 584..586 FT /note="Allosteric activator fructose 2,6-bisphosphate FT binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT REGION 676..679 FT /note="Allosteric activator fructose 2,6-bisphosphate FT binding" 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 METAL 119 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 25 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 201 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 265 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 293 FT /note="Substrate; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 482 FT /note="Allosteric activator fructose 2,6-bisphosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 577 FT /note="Allosteric activator fructose 2,6-bisphosphate; FT shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 644 FT /note="Allosteric activator fructose 2,6-bisphosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 670 FT /note="Allosteric activator fructose 2,6-bisphosphate; FT shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" FT BINDING 755 FT /note="Allosteric activator fructose 2,6-bisphosphate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184" SQ SEQUENCE 805 AA; 87746 MW; 0917EBE117C1702F CRC64; MAGPATTTPV SVSKRRRIAV LTSGGDAPGM NGVVRAVIRM SIHCGCEAYA VHEGYEGLVQ GGDLIKRMHW EDVRGWLSRG GTLIGSARSM SFLTREGRVQ AAKNLVIRGI DALVVCGGDG SLTGADIFRG EWPGLLNELV NKGDLTAEQA EPYTCLNIVG IVGSIDNDMS TTDATVGCYS SLHRICEAVD EVFDTAASHQ RGFVIEVMGR HCGWLALMSA ISTGADWLFI PERPPRDGWE DDMCDIITQQ NRKRGKRRTI VIVAEGAQDT NLKKITSESV KELLSNRLKL DTRVTVLGHT QRGGPACAYD RWLGTLQGIE AVKAVLEAKP GSPSPIITIR ENKIERSSLV EAVRVTRTVT QAIKEKDFAT AMDMRDAEFK AYHRAYINTT TPHHPKLQLP SDKRMRIAII HVGAPAGGMN PATRAAVAYC LARGHTPIAI YNGFPGLCRH HADKPLGSVR IVKWLESDSW VNEGGSEIGT NRGLPSEDMP KTAECFELYK FDALFVIGGF EAFTAVSQLR KAREQYPAFR IPLVVLPATI SNNVPGTEYS LGSDTCLNTL VTFCDVIRQS ASSSRRRVFV IETQGGRSGY IATMAGLAIG AFAVYIPEEG IDIKMLARDI EYLRRNFATD RGASHAGKII LRNERASGTY TTQVIADMIK EEARGRFESR AAVPGHFQQG GKPSPMDRVR ALRMAIKCIQ HMETFFGRSG ESIAADPMSS VVIGIKGSEV VFGPMGPGAD GLGGLEETDT DWVHRRPKND FWMGLKDLVD TLSGRPGEDH PGVLRMADEE GWGAYAPVDP CHFTE //