ID Q6SYC5_ASCSU Unreviewed; 812 AA.
AC Q6SYC5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 95.
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};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:AAR16088.1};
RN [1] {ECO:0000313|EMBL:AAR16088.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16108551; DOI=10.1645/GE-369R;
RA Kulkarni G., Sabnis N.A., Bhat K.S., Harris B.G.;
RT "Cloning and nucleotide sequence of a full-length cDNA encoding Ascaris
RT suum phosphofructokinase.";
RL J. Parasitol. 91:585-590(2005).
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|ARBA:ARBA00002659, ECO:0000256|HAMAP-
CC 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,
CC 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|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_03184,
CC 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03184}.
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DR EMBL; AY445522; AAR16088.1; -; mRNA.
DR AlphaFoldDB; Q6SYC5; -.
DR SMR; Q6SYC5; -.
DR SABIO-RK; Q6SYC5; -.
DR UniPathway; UPA00109; UER00182.
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 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; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR PANTHER; PTHR13697:SF4; 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.
PE 2: Evidence at transcript level;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW Rule:MF_03184};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03184};
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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03184};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03184}.
FT DOMAIN 49..354
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT DOMAIN 438..722
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT REGION 1..421
FT /note="N-terminal catalytic PFK domain 1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT REGION 438..812
FT /note="C-terminal regulatory PFK domain 2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 119..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 149..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 195..197
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 232
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 239..241
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 295
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 323
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03184"
FT BINDING 329..332
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 507
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 564..568
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 602
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 609..611
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 665
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 691
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 697..700
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 773
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 812 AA; 88778 MW; D8B139D1276818F6 CRC64;
MSVEDSVGPL PDMNAPRARF AKGRSDSIVP TAGKEGSIIV PHLYKGQSIA VFTSGGDAPG
MNSAVRSVVR MGIYLGCRVY FIYEGYQGMV DGGDNIKEAD WNSVSDIIRK GGTIIGTERG
KEFREREGRL RAAENLIAHN ITNLVCIGGD GSLTGANLFR QEWPGLVKDL LAAGRITAEK
AQQCANIQIV GLVGSIDNDF CGTDMTIGTD TALQRIIEAI DSVMSTAQSH QRCFVIEVMG
RHCGYLAVVA ALASEADFCF IPEWPAPTDW PDVLCKKLQT MRAEGQRLNI IIVAEGAIDR
EGKAITAEIV RGVVKSTLHY DTRVTVLGHV QRGGSPSAFD RLLGCRMGAE AVLALMEMTP
ESEPCLVSID GNLMVRVPLM QCVLRTQAVQ KAMDARDWET AVKLRGRSFQ RNLETYRLLT
KLHIPKEKDN LSAGHKFNVA VINVGAPAGG MNAAVRSFVR MAIYHHCRVY GVQNSFEGLA
RGDLKEMAWS DVNNWVMHGG SFLGTQKQLP DKSMPEVAAV LAKFNIHAIL LVGGFEAYHS
CLLLSRARSI YPSLRIPMCI IPCTISNNIP GTSLSLGSDT AVNEICHMID KIKQSATGTK
RRVFIVETMG GYCGYLATLS ALASGADNAY IFEEKFGVLD ILEDVKVITK KMEKGVQRYL
IVRCELANRN YTTEFVKQLF AEEGKGAFST RTNVLGHAQQ GGSPTPFDRN LGTKLAARAL
EYLVTQAKEA INLKTGVASA TNADTATLLG LRGRRVVFTP VEELALETDF EHRLPKEQWW
LKVRPLLRIL AQHDSIYEAE SMAVPECEGE IN
//