ID A0A2V0MYL4_9MYCO Unreviewed; 343 AA. AC A0A2V0MYL4; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 13-NOV-2019, 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 ECO:0000313|EMBL:GBE66350.1}; GN ORFNames=MFM001_28120 {ECO:0000313|EMBL:GBE66350.1}; OS Mycobacterium sp. MFM001. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; unclassified Mycobacterium. OX NCBI_TaxID=2049453 {ECO:0000313|EMBL:GBE66350.1, ECO:0000313|Proteomes:UP000256682}; RN [1] {ECO:0000313|EMBL:GBE66350.1, ECO:0000313|Proteomes:UP000256682} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MFM001 {ECO:0000313|EMBL:GBE66350.1, RC ECO:0000313|Proteomes:UP000256682}; RX PubMed=29885807; DOI=10.1016/j.vetmic.2018.05.010; RA Kayanuma H., Ogihara K., Yoshida S., Yamamoto K., Wada T., RA Yamamoto T., Tsuyuki Y., Madarame H.; RT "Disseminated nontuberculous mycobacterial disease in a cat caused by RT Mycobacterium sp. strain MFM001."; RL Vet. Microbiol. 220:90-96(2018). 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: 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: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:SAAS00609123}; 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:SAAS00041065}. 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:SAAS00551378}. 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:GBE66350.1}. 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; BFAB01000007; GBE66350.1; -; Genomic_DNA. DR UniPathway; UPA00109; UER00182. DR Proteomes; UP000256682; 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:UP000256682}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436108}; KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436111}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436062, ECO:0000313|EMBL:GBE66350.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436079}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436116}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01976}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01976, KW ECO:0000256|SAAS:SAAS00436075}. FT DOMAIN 2 298 PFK. {ECO:0000259|Pfam:PF00365}. FT NP_BIND 73 74 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT NP_BIND 103 106 ATP. {ECO:0000256|HAMAP-Rule:MF_01976}. FT REGION 126 128 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 170 172 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT REGION 273 276 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_01976}. FT ACT_SITE 128 128 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT METAL 104 104 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 163 163 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT BINDING 223 223 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_01976}. FT BINDING 267 267 Substrate; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_01976}. FT SITE 105 105 Important for substrate specificity; FT cannot use PPi as phosphoryl donor. FT {ECO:0000256|HAMAP-Rule:MF_01976}. SQ SEQUENCE 343 AA; 37072 MW; 95CB6F1189D0CECB CRC64; MRIGVLTGGG DCPGLNAVIR AVVRTCDARY GSSVVGFQDG WRGLLENRRI QLHNDDRNDR LLSKGGTMLG TARVHPDKLR AGLPQIMQTL DDNGIDVLIP IGGEGTLTAA HWLSEENVPV VGVPKTIDND IDCTDVTFGH DTALTVATDA IDRLHSTAES HQRVMLVEVM GRHAGWIALN AGLASGAHMT LIPEQPFDVE EVCRLVKRRF QRGDSHFVCV VAEGAKPIPG SMMLREGGMD EFGHERFTGV ATQLAAEVEK RINKDVRVTV LGHVQRGGTP TAYDRVLATR FGVNAADAAH AGEYGQMVSL RGQDIGRVPL ADAVRQLKLV PQSRYDDAAA FFG //