PFKA_AMYME
ID PFKA_AMYME Reviewed; 459 AA.
AC Q8VU09;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01981};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_01981};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01981};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01981};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_01981};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_01981}; Synonyms=pfk;
OS Amycolatopsis methanolica.
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1814;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-28 AND 423-451,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP SUBUNIT, AND ACTIVITY REGULATION.
RC STRAIN=DSM 44096 / JCM 8087 / NBRC 15065 / NCIMB 11946 / NRRL B-24139 / LMD
RC 80.32 / 239;
RX PubMed=11717283; DOI=10.1128/jb.183.24.7231-7240.2001;
RA Alves A.M., Euverink G.J., Santos H., Dijkhuizen L.;
RT "Different physiological roles of ATP- and PP(i)-dependent
RT phosphofructokinase isoenzymes in the methylotrophic actinomycete
RT Amycolatopsis methanolica.";
RL J. Bacteriol. 183:7231-7240(2001).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000255|HAMAP-Rule:MF_01981,
CC ECO:0000269|PubMed:11717283}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC ChEBI:CHEBI:456216; EC=2.7.1.11; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01981, ECO:0000269|PubMed:11717283};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01981,
CC ECO:0000269|PubMed:11717283};
CC -!- ACTIVITY REGULATION: AMP causes 20-40% inhibition and diphosphate
CC causes 20-50% inhibition. ADP, citrate, PEP and FBP have no effect.
CC {ECO:0000269|PubMed:11717283}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.6 mM for ATP {ECO:0000269|PubMed:11717283};
CC Vmax=180 umol/min/mg enzyme {ECO:0000269|PubMed:11717283};
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_01981}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01981,
CC ECO:0000269|PubMed:11717283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01981}.
CC -!- INDUCTION: Present when grown on one-carbon (C(1)) compounds.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_01981}.
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DR EMBL; AF298119; AAL39011.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VU09; -.
DR SMR; Q8VU09; -.
DR PRIDE; Q8VU09; -.
DR BRENDA; 2.7.1.11; 314.
DR SABIO-RK; Q8VU09; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR012004; PyroP-dep_PFK_TP0108.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Nucleotide-binding; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11717283"
FT CHAIN 2..459
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000429712"
FT ACT_SITE 210
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 154..155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 179..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 180
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 253..255
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT BINDING 368..371
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT SITE 181
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01981"
FT CONFLICT 16
FT /note="C -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..27
FT /note="LS -> HT (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 48934 MW; B2A92A873A15A7AC CRC64;
MTLHLDDLRV RLLGECRYDS PFAEVLSTKR TSPHYVAEGD RVLLEDTVAM LAEHSLPSVQ
APSFEAAGPR RKIYFDPARV TAGIVTCGGL CPGLNNVIRG LVQELSVHYR VKRIVGFRNG
PGLTAAHRDD TVELTPEVVR DIHNLGGTIL GSSRGGQDAD EMVETLALHG VDVMFVIGGD
GGMRAATFLS GAIRARGLDI AVIGVPKTID NDLPFTDQSF GFQSAFARAT DFISAVSVEA
AASPNGVGIV KLMGRHSGFI AAYAALAANS ADVVLIPEVP FALDGDDGLL AHVERLVRAK
GFAVVVVAEG AGQDLFDAHG LPQLNGRGTD ASGNVKLGNI GELLRTSIEA HLTAAGLAPT
MRYIDPSYAI RSIPANAYDS VYCLRLAHAA VHAAMAGRTE AAVARWRRRF VHVPFSLMTR
RRNQVDPDGD LWMSVLETTC QPAEFGAVAA RERISSGFC
