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LOCUS WP_011217049 320 aa linear BCT 03-JUN-2024 ACCESSION WP_011217049 VERSION WP_011217049.1 KEYWORDS RefSeq. SOURCE Photobacterium profundum ORGANISM Photobacterium profundum Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; Photobacterium. 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="Photobacterium profundum" /db_xref="taxon:74109" 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=34653 Region 2..320 /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..319) /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 vrgvvraals dglevygiyd gyqglhqnri eklsrtsvsd 61 vinrggtflg sarfpefkde kvraqaiqnl kmhgiealvv iggdgsymga kkltemgfpc 121 igipgtidnd vagtdytigy ftalntvida idrlrdtsss hqrisivevm grhcgdltlm 181 saiaggceyi itpetglhke eliakikegi ykgkkhaiva ltelmtdane lakyiedetg 241 retratvlgh iqrggqptaf drilasrmga yavelliqge ggrcvgvqne kmvhhdiida 301 ienmkrpvrk dlyeladklf