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LOCUS WP_002882911 320 aa linear BCT 03-JUN-2024 ACCESSION WP_002882911 VERSION WP_002882911.1 KEYWORDS RefSeq. SOURCE Gammaproteobacteria ORGANISM Gammaproteobacteria Bacteria; Pseudomonadati; Pseudomonadota. REFERENCE 1 (residues 1 to 320) 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 320) 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 320) 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..320 /organism="Gammaproteobacteria" /db_xref="taxon:1236" gene 1..320 /gene="pfkA" Protein 1..320 /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=34853 Region 2..319 /region_name="PRK03202" /note="ATP-dependent 6-phosphofructokinase" /db_xref="CDD:235111" Site order(12,42,73,104..106,108..109,126,128,130,170..172,223, 250,253) /site_type="active" /db_xref="CDD:238388" Site order(12,42,73,104..106,108..109) /site_type="other" /note="ADP/pyrophosphate binding site [chemical binding]" /db_xref="CDD:238388" Site order(22,26,55,60,63,136,148,152,155,183..184,186,214, 262..263,267,274,289,318..320) /site_type="other" /note="dimerization interface [polypeptide binding]" /db_xref="CDD:238388" Site order(22,26,55..56,59..60,155,186,188,212,214..216) /site_type="active" /note="allosteric effector site [active]" /db_xref="CDD:238388" Site order(126,128,130,163,170..172,223,244,250,253) /site_type="other" /note="fructose-1,6-bisphosphate binding site" /db_xref="CDD:238388" ORIGIN 1 mikkigvlts ggdapgmnaa irgvvraalt eglevfgiyd gylglyedrm vqldrysvsd 61 minrggtflg sarfpefree hiravaienm kkrgldalvv iggdgsymga mrltemgfpc 121 iglpgtidnd ikgtdytigf ftalstvvea idrlrdtsss hqrisvvevm grycgdltla 181 aaiaggcefi mvpeveytrd dlvaeikagi akgkkhaiva itehmcdvde lasyieketg 241 retratvlgh iqrggspvpy drilasrmga yaielllqgh ggrcvgiqne klvhhdiida 301 ienmkrpfkn dwldcakkly