PFKA2_CAEEL
ID PFKA2_CAEEL Reviewed; 756 AA.
AC Q27483;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ATP-dependent 6-phosphofructokinase 2;
DE Short=ATP-PFK 2;
DE Short=Phosphofructokinase 2;
DE EC=2.7.1.11 {ECO:0000250|UniProtKB:P16861};
DE AltName: Full=Phosphohexokinase 2;
GN Name=pfk-1.2 {ECO:0000312|WormBase:C50F4.2};
GN ORFNames=C50F4.2 {ECO:0000312|WormBase:C50F4.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:0000250|UniProtKB:P16861}.
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:0000250|UniProtKB:P16861};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P16861};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000250|UniProtKB:P16861}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000250|UniProtKB:P16861}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P16861}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P16861}.
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:0000305}.
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DR EMBL; Z70750; CAA94737.1; -; Genomic_DNA.
DR PIR; T20109; T20109.
DR RefSeq; NP_505457.1; NM_073056.3.
DR AlphaFoldDB; Q27483; -.
DR SMR; Q27483; -.
DR STRING; 6239.C50F4.2; -.
DR EPD; Q27483; -.
DR PaxDb; Q27483; -.
DR PeptideAtlas; Q27483; -.
DR PRIDE; Q27483; -.
DR EnsemblMetazoa; C50F4.2.1; C50F4.2.1; WBGene00008230.
DR GeneID; 179335; -.
DR KEGG; cel:CELE_C50F4.2; -.
DR UCSC; C50F4.2; c. elegans.
DR CTD; 179335; -.
DR WormBase; C50F4.2; CE05467; WBGene00008230; pfk-1.2.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; Q27483; -.
DR OMA; RCYLIRE; -.
DR OrthoDB; 172878at2759; -.
DR PhylomeDB; Q27483; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-70171; Glycolysis.
DR UniPathway; UPA00109; UER00182.
DR PRO; PR:Q27483; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00008230; Expressed in larva and 1 other tissue.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.460; -; 2.
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; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..756
FT /note="ATP-dependent 6-phosphofructokinase 2"
FT /id="PRO_0000112029"
FT REGION 1..393
FT /note="N-terminal catalytic PFK domain 1"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT REGION 394..404
FT /note="Interdomain linker"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT REGION 405..756
FT /note="C-terminal regulatory PFK domain 2"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 81..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 111..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 157..159
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 194
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 201..203
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 257
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 285
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 291..294
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P16861"
FT BINDING 474
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:0000250|UniProtKB:P16861"
FT BINDING 530..534
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:0000250|UniProtKB:P16861"
FT BINDING 575..577
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:0000250|UniProtKB:P16861"
FT BINDING 632
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:0000250|UniProtKB:P16861"
FT BINDING 658
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:0000250|UniProtKB:P16861"
FT BINDING 664..667
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:0000250|UniProtKB:P16861"
SQ SEQUENCE 756 AA; 83301 MW; 26A89B801D286534 CRC64;
MEQKFKKGKD HGVGVLTSGG DSQGMNAAVR SVVRETIRQG HRCYLIREGY NGLINGNIEL
AKWAHVANVT HLGGSMIGTS RCDEFRTTDG RKKAAAIMFD KRIFHLIVIG GDGSLMGAQK
LKEEWGRFGE ELFAEGKITE EVANEGRELH LAGIVGSIDN DCIESDKSIG SDTALHRICE
AIDGLVMTAQ SHQRVFVVEV MGRHCGYLAL TAAIAVEADY VFYPEIPPDE KWPEQLCHQL
GSVRKMGKRQ NVIILGEGVT NSKGQRIDVR QVKEEIETRL QLEVRIATLG HLQRGGAPSF
LDRLIGLRMG YEAVQEVLKG KEEKEGAVVT GQKTIAKVMC LRGHNIQRNE LSRVIRQTET
ANEEIMQRHS DLACRLRGFG FLDKQTYLNF VSIPLSTTMP SRTKTFAVVH IGSPCAGMNA
ATYSFTRMAN HSGIQVIGIK HGWDGLKNKD VKLLTWANVQ GWAQFGGSML GTKRQLPSEM
DLIAEGLNSN NVDGLVIIGG FMAFESALIL QQNRSEYTCL SIPIVVIPAT ISNNCPGTCM
SLGVDTALNE ICRQVDNISQ NAIGSKNKVM IIETMGSRSG FLATMTALST GSQFALIRQV
ETNEKDLEKL AIETKERLDS GNLEKFLLIR SEGASDEIYS PDVKKIFDKV MKNKYGVRIT
NLGYSQLGGH PSCFDRQMGI RMGVRAFEGI VNPVKMGDRD CCVIGLRGSS LRYVPVQGLG
KKVCFEHGVP HNMWWLDLHP LVEAMTKKPQ EAVLSS
