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ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase)

 A0A084FVT2_9PEZI        Unreviewed;       785 AA.
A0A084FVT2;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
25-OCT-2017, entry version 20.
RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184};
Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03184};
Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03184};
EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03184};
AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03184};
ORFNames=SAPIO_CDS9854 {ECO:0000313|EMBL:KEZ39194.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ39194.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ39194.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ39194.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
to fructose 1,6-bisphosphate by ATP, the first committing step of
glycolysis. {ECO:0000256|HAMAP-Rule:MF_03184}.
-!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03184,
ECO:0000256|PIRNR:PIRNR000533}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03184};
-!- ENZYME REGULATION: Allosterically activated by ADP, AMP, or
fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
citrate. {ECO:0000256|HAMAP-Rule:MF_03184}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_03184, ECO:0000256|PIRNR:PIRNR000533}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03184}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
clade "E" sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03184,
ECO:0000256|PIRNR:PIRNR000533}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_03184}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ39194.1}.
-----------------------------------------------------------------------
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EMBL; JOWA01000154; KEZ39194.1; -; Genomic_DNA.
RefSeq; XP_016638993.1; XM_016791149.1.
EnsemblFungi; KEZ39194; KEZ39194; SAPIO_CDS9854.
GeneID; 27728926; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000028545; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
InterPro; IPR009161; 6-Pfructokinase_euk.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR015912; Phosphofructokinase_CS.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR035966; PKF_sf.
Pfam; PF00365; PFK; 2.
PIRSF; PIRSF000533; ATP_PFK_euk; 1.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 2.
TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
3: Inferred from homology;
Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03184};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03184,
ECO:0000256|PIRNR:PIRNR000533};
Complete proteome {ECO:0000313|Proteomes:UP000028545};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_03184,
ECO:0000256|PIRNR:PIRNR000533};
Kinase {ECO:0000256|HAMAP-Rule:MF_03184,
ECO:0000256|PIRNR:PIRNR000533, ECO:0000313|EMBL:KEZ39194.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03184};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03184};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03184,
ECO:0000256|PIRNR:PIRNR000533};
Reference proteome {ECO:0000313|Proteomes:UP000028545};
Transferase {ECO:0000256|HAMAP-Rule:MF_03184,
ECO:0000256|PIRNR:PIRNR000533, ECO:0000313|EMBL:KEZ39194.1}.
DOMAIN 8 316 PFK. {ECO:0000259|Pfam:PF00365}.
DOMAIN 399 695 PFK. {ECO:0000259|Pfam:PF00365}.
NP_BIND 79 80 ATP. {ECO:0000256|HAMAP-Rule:MF_03184}.
NP_BIND 109 112 ATP. {ECO:0000256|HAMAP-Rule:MF_03184}.
REGION 1 383 N-terminal catalytic PFK domain 1.
{ECO:0000256|HAMAP-Rule:MF_03184}.
REGION 155 157 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03184}.
REGION 199 201 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03184}.
REGION 291 294 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03184}.
REGION 399 785 C-terminal regulatory PFK domain 2.
{ECO:0000256|HAMAP-Rule:MF_03184}.
REGION 533 537 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000256|HAMAP-
Rule:MF_03184}.
REGION 578 580 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000256|HAMAP-
Rule:MF_03184}.
REGION 670 673 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000256|HAMAP-
Rule:MF_03184}.
ACT_SITE 157 157 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03184}.
METAL 110 110 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03184}.
BINDING 16 16 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03184}.
BINDING 192 192 Substrate; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_03184}.
BINDING 255 255 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03184}.
BINDING 285 285 Substrate; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_03184}.
BINDING 475 475 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000256|HAMAP-
Rule:MF_03184}.
BINDING 571 571 Allosteric activator fructose 2,6-
bisphosphate; shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_03184}.
BINDING 638 638 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000256|HAMAP-
Rule:MF_03184}.
BINDING 664 664 Allosteric activator fructose 2,6-
bisphosphate; shared with dimeric
partner. {ECO:0000256|HAMAP-
Rule:MF_03184}.
BINDING 742 742 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000256|HAMAP-
Rule:MF_03184}.
SEQUENCE 785 AA; 86071 MW; A77167A9276B19B6 CRC64;
MAEPHKKRIA VMTSGGDSPG MCGVVRAVVR MAIHLNCDAY CVYEGYEGLV QGGKFIRQMQ
WHEVRGWLSE GGTLIGTARC KAFFEREGRL VAAKNMILNG IDALIICGGD GSLTGADKFR
SEWPSLIEEL VQTGQFTQEQ VDPFKHLNIV GIVGSIDNDM SGTDATIGAY SALSRICEMV
DYIEATAYSH SRAFVIEVMG RHCGWLALMA GVATGADFIF IPERPRGDDW QSEMCDIIRR
HRKLGKRKTI VIIAEGALDA QGEKITPEMV KDLLADKNGL ALDTRITTLG HVQRGGTAVS
YDRMLATLQG VEAVKAVLDA TPETPTCFIA INENKIVRKN LMEAVKDTKE VAAAVQAKDF
DRAMSLRDHE FLDQYKSYMM TTNVHMDDGE KVPEIQRMKI AFINVGAPAG AMNAAIRAGV
AYCISRGHEP IAIHNGFAGF ARHHGDKPIG AVRSFDWLEV DSWASKGGSE IGTNRELPAD
SGMETIANLI EQYRFDALFL IGGFEAFHAV SQLRAARDEY PSLCIPMCIL PATISNNVPG
TEYSLGSDTC LNELVNYCDK IKQSASATRR RVFVIETQGG KSGYVATLAG LTVGASAVYT
PEEGISLDML AADVKHLKEV FKKDRGQSRA GRLLLVNEKA SKVYTAKLIA DIIREEANER
FESRDSIPGH VQQGGVPSPI DRCRAVRLAI KCIEHLESFG RRAQNKVKHD PYSTVVIGIR
GASVVFTPVA ELEETDTDWP NRRPITSHWA GLKDIVDVLG GRNPYPKPEH KLTGLKAKDT
KRGLR


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