ID A0A1J9P7U8_9EURO Unreviewed; 805 AA. AC A0A1J9P7U8; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 10-MAY-2017, entry version 4. 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 pasteuriana 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 CC to fructose 1,6-bisphosphate by ATP, the first committing step of CC glycolysis. {ECO:0000256|HAMAP-Rule:MF_03184}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03184, CC ECO:0000256|PIRNR:PIRNR000533}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_03184}; CC -!- ENZYME REGULATION: Allosterically activated by ADP, AMP, or CC fructose 2,6-bisphosphate, and allosterically inhibited by ATP or CC citrate. {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) CC family. ATP-dependent PFK group I subfamily. Eukaryotic two domain CC clade "E" sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03184, CC ECO:0000256|PIRNR:PIRNR000533}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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-HAMAP. 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 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 Complete proteome {ECO:0000313|Proteomes:UP000182235}; 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, KW ECO:0000256|PIRNR:PIRNR000533, ECO:0000313|EMBL:OJD12174.1}; KW 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 PFK. {ECO:0000259|Pfam:PF00365}. FT DOMAIN 406 701 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 88 89 ATP. {ECO:0000256|HAMAP-Rule:MF_03184}. FT NP_BIND 118 121 ATP. {ECO:0000256|HAMAP-Rule:MF_03184}. FT REGION 1 391 N-terminal catalytic PFK domain 1. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT REGION 164 166 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 208 210 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 299 302 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 392 405 Interdomain linker. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 406 805 C-terminal regulatory PFK domain 2. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT REGION 539 543 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 584 586 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT REGION 676 679 Allosteric activator fructose 2,6- FT bisphosphate binding. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT ACT_SITE 166 166 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT METAL 119 119 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_03184}. FT BINDING 25 25 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT BINDING 201 201 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT BINDING 265 265 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 293 293 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_03184}. FT BINDING 482 482 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 577 577 Allosteric activator fructose 2,6- FT bisphosphate; shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 644 644 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 670 670 Allosteric activator fructose 2,6- FT bisphosphate; shared with dimeric FT partner. {ECO:0000256|HAMAP-Rule: FT MF_03184}. FT BINDING 755 755 Allosteric activator fructose 2,6- FT bisphosphate. {ECO:0000256|HAMAP-Rule: FT 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 //