(data stored in SCRATCH9089 zone)

SWISSPROT: PFKA_PASMU

ID   PFKA_PASMU              Reviewed;         321 AA.
AC   Q9CPH2;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 114.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_00339};
DE            Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339};
GN   Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339}; OrderedLocusNames=PM0069;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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_00339}.
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_00339};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00339};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC       diphosphonucleosides, and allosterically inhibited by
CC       phosphoenolpyruvate. {ECO:0000255|HAMAP-Rule:MF_00339}.
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_00339}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00339}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00339}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00339}.
DR   EMBL; AE004439; AAK02153.1; -; Genomic_DNA.
DR   RefSeq; WP_005751062.1; NC_002663.1.
DR   SMR; Q9CPH2; -.
DR   EnsemblBacteria; AAK02153; AAK02153; PM0069.
DR   GeneID; 29389401; -.
DR   KEGG; pmu:PM0069; -.
DR   eggNOG; ENOG4105CTQ; Bacteria.
DR   eggNOG; COG0205; LUCA.
DR   HOGENOM; HOG000248870; -.
DR   KO; K00850; -.
DR   OMA; RDGWRGP; -.
DR   BioCyc; PMUL272843:G1FZ8-73-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000000809; Chromosome.
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   CDD; cd00763; Bacterial_PFK; 1.
DR   HAMAP; MF_00339; Phosphofructokinase_I_B1; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR012828; PFKA_ATP_prok.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
DR   TIGRFAMs; TIGR02482; PFKA_ATP; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9CPH2.
DR   SWISS-2DPAGE; Q9CPH2.
KW   Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..321
FT                   /note="ATP-dependent 6-phosphofructokinase"
FT                   /id="PRO_0000111971"
FT   NP_BIND         73..74
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   NP_BIND         103..106
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   REGION          22..26
FT                   /note="Allosteric activator ADP binding; shared with
FT                   dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   REGION          55..60
FT                   /note="Allosteric activator ADP binding; shared with
FT                   dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   REGION          127..129
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   REGION          171..173
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   REGION          187..189
FT                   /note="Allosteric activator ADP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   REGION          215..217
FT                   /note="Allosteric activator ADP binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   REGION          251..254
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   ACT_SITE        129
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   METAL           104
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         12
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         156
FT                   /note="Allosteric activator ADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         164
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         213
FT                   /note="Allosteric activator ADP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         224
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT   BINDING         245
FT                   /note="Substrate; shared with dimeric partner"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
SQ   SEQUENCE   321 AA;  35025 MW;  4B71609FECCAC91D CRC64;
     MIKKIAVLTS GGDAPGMNAA IRGVVRSALA AGLEVYGIYE GYYGLYHNKV KQMTRYSVSD
     IINRGGTFLG SARFPEFKDP AVRAKCAEIL RSHGIDALVV IGGDGSYMGA KLLTEEHGFP
     CVGIPGTIDN DVAGTDYTIG YQTALQTAVE AIDRLRDTSS SHQRISIVEI MGRHCSDLAI
     SAGIAGGCEY IVASEVEFNR EELIQQIERS IIKGKRHAII AITELICDVN ELAREIESRV
     KHETRATILG HIQRGGTPCA FDRILGSRMG VYAVDLLMQG KGGYCVGIQN EQLVHHDIID
     AINNMRREFK ADWLALSKRL D
//

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