ID A0A1B9VNQ5_9PROT Unreviewed; 368 AA. AC A0A1B9VNQ5; DT 02-NOV-2016, integrated into UniProtKB/TrEMBL. DT 02-NOV-2016, sequence version 1. DT 27-SEP-2017, entry version 7. 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=KO164_4261 {ECO:0000313|EMBL:OCK10079.1}; OS Thalassospira sp. KO164. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales; OC Rhodospirillaceae; Thalassospira. OX NCBI_TaxID=1798192 {ECO:0000313|EMBL:OCK10079.1, ECO:0000313|Proteomes:UP000093204}; RN [1] {ECO:0000313|EMBL:OCK10079.1, ECO:0000313|Proteomes:UP000093204} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KO164 {ECO:0000313|EMBL:OCK10079.1, RC ECO:0000313|Proteomes:UP000093204}; RA Hazen T., Woo H., Brown S., Utturkar S., Huntemann M., Clum A., RA Pillay M., Palaniappan K., Varghese N., Mikhailova N., Stamatis D., RA Reddy T., Ngan C.Y., Daum C., Shapiro N., Markowitz V., Ivanova N., RA Kyrpides N., Woyke T.; RT "Draft Genome Sequences for Thalassospira sp. KO164."; RL Submitted (JUN-2016) 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:OCK10079.1}. 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; MAJC01000002; OCK10079.1; -; Genomic_DNA. DR RefSeq; WP_007091088.1; NZ_MAJC01000002.1. DR EnsemblBacteria; OCK10079; OCK10079; KO164_4261. DR GeneID; 31928597; -. DR PATRIC; fig|1798192.3.peg.4538; -. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000093204; 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 Pfam; PF00365; PFK; 1. DR PIRSF; PIRSF000532; ATP_PFK_prok; 1. DR PRINTS; PR00476; PHFRCTKINASE. DR SUPFAM; SSF53784; SSF53784; 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:UP000093204}; 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:OCK10079.1}; 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 Transferase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00640113, ECO:0000313|EMBL:OCK10079.1}. FT DOMAIN 2 307 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 76 77 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT NP_BIND 113 116 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT REGION 137 139 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 181 183 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 281 284 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT ACT_SITE 139 139 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT METAL 114 114 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 174 174 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 234 234 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT BINDING 275 275 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 115 115 Important for substrate specificity; FT cannot use PPi as phosphoryl donor. FT {ECO:0000256|HAMAP-Rule:MF_01976}. SQ SEQUENCE 368 AA; 38954 MW; 2A3F530078979B2F CRC64; MRIGILTSGG DCAGLNAVIL AVVRRAVLGY GWDVVGIRQG THGLMQDPPQ AIDLNDYVNN DGMLRLGGTI LGTVNKGDPF HYPMPDGSFA DRSADVIAGY HKLGLDALIG VGGDGSMAIL HRLAEMGGIN LVGIPKTIDN DLALTEYSVG FTTAVNVAVE ALDRLQPTAA SHDRIMILEV MGRDAGHIAL FAGVAGGADA ILIPEMDYDL DALTEHCLNI RKRGRNHALV IVAEAVKRDD GAAVTQGDDG QKIRYGGIGH WLADELGART GWETRVTVLG HVQRGGIPSP RDRVIASAFG VHAVDLIAQK RFDRVVAWSK RKVIDVAMAD VIVGPRLVDT KGTMVSTAKG LGAYLGHPPE TARTAKTV //