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Database: UniProt
Entry: Q6SYC5_ASCSU
LinkDB: Q6SYC5_ASCSU
Original site: Q6SYC5_ASCSU 
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
//
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