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Database: UniProt
Entry: A9WCU2
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ID   PFKA_CHLAA              Reviewed;         356 AA.
AC   A9WCU2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   26-NOV-2014, entry version 52.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_01976};
DE            Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE            EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01976};
DE   AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_01976};
GN   Name=pfkA {ECO:0000255|HAMAP-Rule:MF_01976};
GN   OrderedLocusNames=Caur_0258;
OS   Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=324602;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29366 / DSM 635 / J-10-fl;
RX   PubMed=21714912; DOI=10.1186/1471-2164-12-334;
RA   Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J.,
RA   Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W.,
RA   Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.;
RT   "Complete genome sequence of the filamentous anoxygenic phototrophic
RT   bacterium Chloroflexus aurantiacus.";
RL   BMC Genomics 12:334-334(2011).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
CC       to fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01976};
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_01976}.
CC   -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-
CC       Rule:MF_01976}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
CC       family. Mixed-substrate PFK group III subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01976}.
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DR   EMBL; CP000909; ABY33511.1; -; Genomic_DNA.
DR   RefSeq; YP_001633900.1; NC_010175.1.
DR   ProteinModelPortal; A9WCU2; -.
DR   STRING; 324602.Caur_0258; -.
DR   EnsemblBacteria; ABY33511; ABY33511; Caur_0258.
DR   GeneID; 5824865; -.
DR   KEGG; cau:Caur_0258; -.
DR   PATRIC; 21411026; VBIChlAur28763_0298.
DR   eggNOG; COG0205; -.
DR   HOGENOM; HOG000248869; -.
DR   InParanoid; A9WCU2; -.
DR   KO; K00850; -.
DR   OMA; HRHRAHA; -.
DR   OrthoDB; EOG644ZRM; -.
DR   BioCyc; CAUR324602:GIXU-261-MONOMER; -.
DR   UniPathway; UPA00109; UER00182.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
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   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR012829; PFK.
DR   InterPro; IPR022953; Phosphofructokinase.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; SSF53784; 1.
DR   TIGRFAMs; TIGR02483; PFK_mixed; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW   Transferase.
FT   CHAIN         1    356       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_1000079308.
FT   NP_BIND      78     79       ATP. {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   NP_BIND     115    118       ATP. {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   REGION      138    140       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      182    184       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   REGION      278    281       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   ACT_SITE    140    140       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   METAL       116    116       Magnesium; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING      15     15       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   BINDING     175    175       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   BINDING     235    235       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01976}.
FT   BINDING     272    272       Substrate; shared with dimeric partner.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
FT   SITE        117    117       Important for substrate specificity;
FT                                cannot use PPi as phosphoryl donor.
FT                                {ECO:0000255|HAMAP-Rule:MF_01976}.
SQ   SEQUENCE   356 AA;  37703 MW;  C8B7B858A07B643C CRC64;
     MASKKQRIGV LTSGGDAPGL NAVIRAVVKS ASGLGWEVIG IHDGFEGLLG TKSYRVLTNA
     DVQGLLPRGG TILRTTNKGH FGPRRSDELS EADPYVRAVK AIEEMGLRAL ITIGGEGTQR
     IALELHKLGA PVIGVPKTID NDLAGTDRTF GFDTALQVAT DAIDRLHTTA ASHNRVMVLE
     VMGRHTGWIA LHAGLAGGAD VILIPEIPFS IERVAEKVMA RDQQGSSFSI IVVAEGARPR
     GGSEMYIAEG RLGGIGHWVG EQLEKLTAKE VRVVVLGHLQ RGGSPSPYDR LLSTRYGAAA
     VQAAARGIYG EMVALRGQDI VTVPLAEACG HLNRVRPHSD LVLCARSLGI AFGDEL
//
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