LOCUS YP_001255855 319 aa linear BCT 27-SEP-2012
DEFINITION 6-phosphofructokinase [Clostridium botulinum A str. ATCC 3502].
ACCESSION YP_001255855
VERSION YP_001255855.1 GI:148381314
DBLINK Project: 61579
BioProject: PRJNA61579
DBSOURCE REFSEQ: accession NC_009495.1
KEYWORDS .
SOURCE Clostridium botulinum A str. ATCC 3502
ORGANISM Clostridium botulinum A str. ATCC 3502
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
REFERENCE 1 (residues 1 to 319)
AUTHORS Sebaihia,M., Peck,M.W., Minton,N.P., Thomson,N.R., Holden,M.T.,
Mitchell,W.J., Carter,A.T., Bentley,S.D., Mason,D.R., Crossman,L.,
Paul,C.J., Ivens,A., Wells-Bennik,M.H., Davis,I.J.,
Cerdeno-Tarraga,A.M., Churcher,C., Quail,M.A., Chillingworth,T.,
Feltwell,T., Fraser,A., Goodhead,I., Hance,Z., Jagels,K., Larke,N.,
Maddison,M., Moule,S., Mungall,K., Norbertczak,H.,
Rabbinowitsch,E., Sanders,M., Simmonds,M., White,B., Whithead,S.
and Parkhill,J.
TITLE Genome sequence of a proteolytic (Group I) Clostridium botulinum
strain Hall A and comparative analysis of the clostridial genomes
JOURNAL Genome Res. 17 (7), 1082-1092 (2007)
PUBMED 17519437
REFERENCE 2 (residues 1 to 319)
CONSRTM NCBI Genome Project
TITLE Direct Submission
JOURNAL Submitted (04-JAN-2007) National Center for Biotechnology
Information, NIH, Bethesda, MD 20894, USA
REFERENCE 3 (residues 1 to 319)
AUTHORS Sebaihia,M.
TITLE Direct Submission
JOURNAL Submitted (21-NOV-2006) Sebaihia M., Sulston Laboratories, Wellcome
Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton,
Cambridge, CB10 1SA, UNITED KINGDOM
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from CAL84932.
Method: conceptual translation.
FEATURES Location/Qualifiers
source 1..319
/organism="Clostridium botulinum A str. ATCC 3502"
/strain="ATCC 3502"
/db_xref="taxon:413999"
Protein 1..319
/product="6-phosphofructokinase"
/EC_number="2.7.1.11"
/calculated_mol_wt=34072
Region 1..319
/region_name="PRK03202"
/note="6-phosphofructokinase; Provisional"
/db_xref="CDD:179553"
Site order(11,41,72,103..105,107..108,125,127,129,169..171,222,
249,252)
/site_type="active"
/db_xref="CDD:29437"
Site order(11,41,72,103..105,107..108)
/site_type="other"
/note="ADP/pyrophosphate binding site [chemical binding]"
/db_xref="CDD:29437"
Site order(21,25,54,59,62,135,147,151,154,182..183,185,213,
261..262,266,273,288,316)
/site_type="other"
/note="dimerization interface [polypeptide binding]"
/db_xref="CDD:29437"
Site order(21,25,54..55,58..59,154,185,187,211,213..215)
/site_type="other"
/note="allosteric effector site"
/db_xref="CDD:29437"
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:29437"
CDS 1..319
/gene="pfkA"
/locus_tag="CBO3373"
/coded_by="complement(NC_009495.1:3607422..3608381)"
/note="catalyzes the formation of D-fructose
1,6-bisphosphate from D-fructose 6-phosphate in
glycolysis"
/transl_table=11
/db_xref="GeneID:5184682"
ORIGIN
1 mrtiavltsg gdapgmnaai ravvrtglek glkvmgiqrg ynglingeif emdthsvsdi
61 iqrggtilrt arceefrteq grekaakilk afgidglvvi ggdgsfhgaq llsklgintv
121 glpgtidndl aytdytigfd tsintvldai nklrdtstsh ervsvvevmg rncgdialyt
181 gvaggaesii ipekeynadk lckqilqgkl kgkmhnlvll aegvgganel akyieevtgi
241 etrstilghi qrggsptcmd rilasrmayk avellisgks srvvgikngk iidmdideal
301 aversfdqel ydiatilsk
//