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PFKA1_CAEEL
ID   PFKA1_CAEEL             Reviewed;         814 AA.
AC   Q9TZL8; Q95X24;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=ATP-PFK 1 {ECO:0000255|HAMAP-Rule:MF_03184};
DE            Short=Phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE   AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
GN   Name=pfk-1.1 {ECO:0000312|WormBase:Y71H10A.1a};
GN   ORFNames=Y71H10A.1 {ECO:0000312|WormBase:Y71H10A.1a};
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:0000255|HAMAP-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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03184};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_03184}.
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DR   EMBL; FO081433; CCD71595.1; -; Genomic_DNA.
DR   PIR; T33481; T33481.
DR   RefSeq; NP_741738.1; NM_171643.3.
DR   AlphaFoldDB; Q9TZL8; -.
DR   SMR; Q9TZL8; -.
DR   BioGRID; 45527; 13.
DR   STRING; 6239.Y71H10A.1a; -.
DR   EPD; Q9TZL8; -.
DR   PaxDb; Q9TZL8; -.
DR   PeptideAtlas; Q9TZL8; -.
DR   EnsemblMetazoa; Y71H10A.1a.1; Y71H10A.1a.1; WBGene00022199.
DR   GeneID; 180583; -.
DR   KEGG; cel:CELE_Y71H10A.1; -.
DR   UCSC; Y71H10A.1b.3; c. elegans.
DR   CTD; 180583; -.
DR   WormBase; Y71H10A.1a; CE28266; WBGene00022199; pfk-1.1.
DR   eggNOG; KOG2440; Eukaryota.
DR   GeneTree; ENSGT00940000171778; -.
DR   HOGENOM; CLU_011053_0_0_1; -.
DR   InParanoid; Q9TZL8; -.
DR   OMA; FEAYHST; -.
DR   OrthoDB; 172878at2759; -.
DR   PhylomeDB; Q9TZL8; -.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-70171; Glycolysis.
DR   UniPathway; UPA00109; UER00182.
DR   PRO; PR:Q9TZL8; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00022199; Expressed in material anatomical entity and 5 other tissues.
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   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   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; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..814
FT                   /note="ATP-dependent 6-phosphofructokinase 1"
FT                   /id="PRO_0000429718"
FT   REGION          1..420
FT                   /note="N-terminal catalytic PFK domain 1"
FT   REGION          421..435
FT                   /note="Interdomain linker"
FT   REGION          436..814
FT                   /note="C-terminal regulatory PFK domain 2"
FT   ACT_SITE        196
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         118..119
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         148..151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         194..196
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         238..240
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         322
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         328..331
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         505
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:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         563..567
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:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         601
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:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         608..610
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:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         664
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:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         690
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:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         696..699
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:0000255|HAMAP-Rule:MF_03184"
FT   BINDING         771
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:0000255|HAMAP-Rule:MF_03184"
SQ   SEQUENCE   814 AA;  89734 MW;  DA829E8969EDF1CE CRC64;
     MDADASTITP EELDFIRQRA LRRFDSIVPT AGREGTEIAS DIFKGRTLAI YTSGGDSQGM
     NSAVRSITRM AIYCGCKVYL IYEGYEGMIE GGDFIKEATW NTVSDIIQQG GTIIGSARSS
     EFRTREGRLK AATNLINRGI GRLVCIGGDG SLTGANTFRL EWTDLVQELV KNQRVTAAAA
     KKIPYIQIVG LVGSIDNDFC GTDMTIGTDS ALQRIISSID AVVATAQSHQ RAFVIEVMGR
     HCGYLALVAA LASEADFCFI PEWPAPENWR DVLCDKLSQM RSEGQRLNII IVAEGAIDRD
     GKAITAEDVK TAVKEKLKYD TRVTILGHVQ RGGAPSAFDR LLGCRMGAEA VFALMEMTEE
     SEPCVISIDG NVMVRVPLLK CVERTQMVQK AMADKDWTTA VMLRGRSFQR NLETYKLLTK
     MRTVEKDNLS EGHKFNVAVI NVGAPAGGMN AAVRSYVRMA LYHQCTVYGI EDSFEGLANG
     SFKQFKWSDV TNWAMNGGSF LGTQKSLPTE KTMPQLAAQL KKHNIQALLL VGGFEAYHST
     IILAENREKY PEFCIPMCVI PCTISNNVPG TMVSLGSDTA INEICQMIDK IKQSATGTKR
     RVFIVETMGG YCGYLATLSA LSSGADNAYI FEEPFTVQDL SDDVDVILSK MEVGAKRYLV
     VRNEWADKNL TTDFVQNLFD SEGKKNFTTR VNVLGHVQQG GSPTPFDRNM GTKLAARALE
     FLLIQLKENL TADNKVIAKS AHTATLLGLK GRKVVFTPVQ DLKKETDFEH RLPSEQWWMA
     LRPLLRVLAR HRSTVESSAI LESVEEESAD SHMF
 
 
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