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LOCUS WP_005089906 314 aa linear BCT 03-JUN-2024 ACCESSION WP_005089906 VERSION WP_005089906.1 KEYWORDS RefSeq. SOURCE Shigella flexneri ORGANISM Shigella flexneri Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Shigella. REFERENCE 1 (residues 1 to 314) 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 314) 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 314) 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..314 /organism="Shigella flexneri" /db_xref="taxon:623" gene 1..314 /gene="pfkA" Protein 1..314 /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=34072 Region 2..313 /region_name="PRK03202" /note="ATP-dependent 6-phosphofructokinase" /db_xref="CDD:235111" Site order(6,36,67,98..100,102..103,120,122,124,164..166,217, 244,247) /site_type="active" /db_xref="CDD:238388" Site order(6,36,67,98..100,102..103) /site_type="other" /note="ADP/pyrophosphate binding site [chemical binding]" /db_xref="CDD:238388" Site order(16,20,49,54,57,130,142,146,149,177..178,180,208, 256..257,261,268,283,312..314) /site_type="other" /note="dimerization interface [polypeptide binding]" /db_xref="CDD:238388" Site order(16,20,49..50,53..54,149,180,182,206,208..210) /site_type="active" /note="allosteric effector site [active]" /db_xref="CDD:238388" Site order(120,122,124,157,164..166,217,238,244,247) /site_type="other" /note="fructose-1,6-bisphosphate binding site" /db_xref="CDD:238388" ORIGIN 1 mltsggdapg mnaairgvvr salteglevm giydgylgly edrmvqldry svsdminrgg 61 tflgsarfpe frdenirava ienlkkrgid alvviggdgs ymgamrltem gfpciglpgt 121 idndikgtdy tigfftalst vveaidrlrd tssshqrisv vevmgrycgd ltlaaaiagg 181 cefvvvpeve fsredlvnei kagiakgkkh aivaitehmc dvdelahfie ketgretrat 241 vlghiqrggs pvpydrilas rmgayaidll lagyggrcvg iqneqlvhhd iidaienmkr 301 pfkgdwldca kkly