ID A0A0W8I0Z1_9MICO Unreviewed; 339 AA. AC A0A0W8I0Z1; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 22-NOV-2017, entry version 16. DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01976}; DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01976}; DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01976}; DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01976}; GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_01976}; GN ORFNames=AVL62_12570 {ECO:0000313|EMBL:KUG51080.1}; OS Serinicoccus chungangensis. OC Bacteria; Actinobacteria; Micrococcales; Intrasporangiaceae; OC Serinicoccus. OX NCBI_TaxID=767452 {ECO:0000313|EMBL:KUG51080.1, ECO:0000313|Proteomes:UP000054837}; RN [1] {ECO:0000313|EMBL:KUG51080.1, ECO:0000313|Proteomes:UP000054837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CD08_5 {ECO:0000313|EMBL:KUG51080.1, RC ECO:0000313|Proteomes:UP000054837}; RA Chander A.M., Kaur G., Nair G.R., Dhawan D.K., Kochhar R.K., RA Mayilraj S., Bhadada S.K.; RT "Serinicoccus chungangenesis strain CD08_5 genome sequencing and RT assembly."; RL Submitted (DEC-2015) 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:0000256|HAMAP-Rule:MF_01976}. CC -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D- CC fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01976, ECO:0000256|SAAS:SAAS00640094}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 3/4. CC {ECO:0000256|HAMAP-Rule:MF_01976, ECO:0000256|SAAS:SAAS00640117}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000256|HAMAP- CC Rule:MF_01976}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976, CC ECO:0000256|SAAS:SAAS00640112}. CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) CC family. Mixed-substrate PFK group III subfamily. CC {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01976}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KUG51080.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LQBL01000033; KUG51080.1; -; Genomic_DNA. DR RefSeq; WP_058892625.1; NZ_LQBL01000033.1. DR EnsemblBacteria; KUG51080; KUG51080; AVL62_12570. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000054837; Unassembled WGS sequence. 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 {ECO:0000256|HAMAP-Rule:MF_01976}; KW Complete proteome {ECO:0000313|Proteomes:UP000054837}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00640104}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00640111}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00640102, ECO:0000313|EMBL:KUG51080.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00640121}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00640110}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976}; KW Reference proteome {ECO:0000313|Proteomes:UP000054837}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00640113}. FT DOMAIN 2 293 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 72 73 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT NP_BIND 101 104 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT REGION 124 126 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 168 170 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 269 272 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT ACT_SITE 126 126 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT METAL 102 102 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT BINDING 10 10 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 161 161 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 220 220 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT BINDING 263 263 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 103 103 Important for substrate specificity; FT cannot use PPi as phosphoryl donor. FT {ECO:0000256|HAMAP-Rule:MF_01976}. SQ SEQUENCE 339 AA; 36186 MW; 7CA5BB9EB35269A9 CRC64; MKIGLLTSGG DCPGLNAVIR GVVLKGDRIY EHEFVGIKDG FRGLVEDDIV PLPRKRVRGL SKVGGTILGT SRISPIRTGG IDRVKEVMDK HEIDALVAIG GEGTLTVARM FHDEGINVVG VPKTIDNDLS ATDRTFGFDT AVSIATESID RLRTTGEAHS RCMVVEVMGR HVGWIALHAG IASGAHAILI PEVPVSSDQL CQWVQNAMDR GRAPTIVVAE GFTFAGAEQV ASDRVDGFGR PLLGGIGEAV TRAIEEHTGI ETRNTTLGHL QRGGVPSSYD RVLATRFGTA AIDSVSAKKW GTMVALSGMD IVNVNLRDAT SELKLVPRDQ WDEAAIMFG //