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 16-JAN-2019, entry version 60.
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:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
CC 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
CC ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
CC Evidence={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; 1421302at2; -.
DR BioCyc; CSP480224:G1GUP-282-MONOMER; -.
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
//
