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LOCUS WP_003723299 319 aa linear BCT 03-JUN-2024 ACCESSION WP_003723299 VERSION WP_003723299.1 KEYWORDS RefSeq. SOURCE Listeria ORGANISM Listeria Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae. REFERENCE 1 (residues 1 to 319) AUTHORS Sakai,H. and Ohta,T. TITLE Molecular cloning and nucleotide sequence of the gene for pyruvate kinase of Bacillus stearothermophilus and the production of the enzyme in Escherichia coli. Evidence that the genes for phosphofructokinase and pyruvate kinase constitute an operon JOURNAL Eur J Biochem 211 (3), 851-859 (1993) PUBMED 8436141 REFERENCE 2 (residues 1 to 319) AUTHORS Le Bras,G., Deville-Bonne,D. and Garel,J.R. TITLE Purification and properties of the phosphofructokinase from Lactobacillus bulgaricus. A non-allosteric analog of the enzyme from Escherichia coli JOURNAL Eur J Biochem 198 (3), 683-687 (1991) PUBMED 1828763 REFERENCE 3 (residues 1 to 319) AUTHORS Hellinga,H.W. and Evans,P.R. TITLE Mutations in the active site of Escherichia coli phosphofructokinase JOURNAL Nature 327 (6121), 437-439 (1987) PUBMED 2953977 COMMENT REFSEQ: This record represents a single, non-redundant, protein sequence which may be annotated on many different RefSeq genomes from the same, or different, species. ##Evidence-For-Name-Assignment-START## Evidence Category :: HMM Evidence Accession :: TIGR02482.1 Evidence Source :: JCVI ##Evidence-For-Name-Assignment-END## COMPLETENESS: full length. FEATURES Location/Qualifiers source 1..319 /organism="Listeria" /db_xref="taxon:1637" gene 1..319 /gene="pfkA" Protein 1..319 /product="6-phosphofructokinase" /EC_number="2.7.1.11" /GO_function="GO:0005524 - ATP binding [Evidence IEA]" /GO_process="GO:0006002 - fructose 6-phosphate metabolic process [Evidence IEA]" /GO_process="GO:0006096 - glycolytic process [Evidence IEA]" /calculated_mol_wt=34289 Region 1..319 /region_name="PRK03202" /note="ATP-dependent 6-phosphofructokinase" /db_xref="CDD:235111" Site order(11,41,72,103..105,107..108,125,127,129,169..171,222, 249,252) /site_type="active" /db_xref="CDD:238388" Site order(11,41,72,103..105,107..108) /site_type="other" /note="ADP/pyrophosphate binding site [chemical binding]" /db_xref="CDD:238388" Site order(21,25,54,59,62,135,147,151,154,182..183,185,213, 261..262,266,273,288,316..318) /site_type="other" /note="dimerization interface [polypeptide binding]" /db_xref="CDD:238388" Site order(21,25,54..55,58..59,154,185,187,211,213..215) /site_type="active" /note="allosteric effector site [active]" /db_xref="CDD:238388" Site order(125,127,129,162,169..171,222,243,249,252) /site_type="other" /note="fructose-1,6-bisphosphate binding site" /db_xref="CDD:238388" ORIGIN 1 mkriailtsg gdapgmnaat ravvrkaiye glevyginyg flglvngdir klelgsvgdl 61 lhrggtflys arypefatee gqlkgieqlk khqidglvvi ggdgsyhgae altkrgfpti 121 gipgtidndi sgtdftigfd talntvldal dkirdtatsh ertfiievmg rdagdialws 181 glaggaeaii vpeesfnmdd vvdrlnkgre rgkkhsiivv aegvmsgnef akqlaeygdy 241 harvtvlghv qrggsptafd rvlasrlgar svelllenrg glavgirenr ivendiseil 301 kekhtldqkl fdlasilsi