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Database: UniProt
Entry: B9LHK4
LinkDB: B9LHK4
Original site: B9LHK4 
ID   PFKA_CHLSY              Reviewed;         356 AA.
AC   B9LHK4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   10-OCT-2018, entry version 58.
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=Chy400_0274;
OS   Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC   Chloroflexaceae; Chloroflexus.
OX   NCBI_TaxID=480224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29364 / DSM 637 / Y-400-fl;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Kiss H.,
RA   Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Ovchinnikova G., Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroflexus sp. Y-400-fl.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP001364; ACM51713.1; -; Genomic_DNA.
DR   RefSeq; WP_012256167.1; NC_012032.1.
DR   ProteinModelPortal; B9LHK4; -.
DR   SMR; B9LHK4; -.
DR   EnsemblBacteria; ACM51713; ACM51713; Chy400_0274.
DR   KEGG; chl:Chy400_0274; -.
DR   HOGENOM; HOG000248869; -.
DR   KO; K21071; -.
DR   OMA; RDGWRGP; -.
DR   OrthoDB; POG091H01AC; -.
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:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR012829; Phosphofructokinase_III.
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; TIGR02483; PFK_mixed; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    356       ATP-dependent 6-phosphofructokinase.
FT                                /FTId=PRO_1000192368.
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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