ID E6BKB1_ECOLX Unreviewed; 312 AA.
AC E6BKB1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE RecName: Full=Phosphofructokinase {ECO:0000256|PIRNR:PIRNR000535};
GN Name=pfkB {ECO:0000313|EMBL:EFU35286.1};
GN ORFNames=HMPREF9350_02718 {ECO:0000313|EMBL:EFU35286.1};
OS Escherichia coli MS 85-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=679202 {ECO:0000313|EMBL:EFU35286.1, ECO:0000313|Proteomes:UP000005056};
RN [1] {ECO:0000313|EMBL:EFU35286.1, ECO:0000313|Proteomes:UP000005056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 85-1 {ECO:0000313|EMBL:EFU35286.1,
RC ECO:0000313|Proteomes:UP000005056};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-
CC phosphate to fructose-l,6-bisphosphate.
CC {ECO:0000256|RuleBase:RU369061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:14213, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:138881,
CC ChEBI:CHEBI:456216; EC=2.7.1.56;
CC Evidence={ECO:0000256|ARBA:ARBA00000823,
CC ECO:0000256|RuleBase:RU369061};
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000256|ARBA:ARBA00010688, ECO:0000256|PIRNR:PIRNR000535,
CC ECO:0000256|RuleBase:RU369061}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFU35286.1}.
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DR EMBL; ADWQ01000010; EFU35286.1; -; Genomic_DNA.
DR RefSeq; WP_000091263.1; NZ_ADWQ01000010.1.
DR AlphaFoldDB; E6BKB1; -.
DR SMR; E6BKB1; -.
DR GeneID; 75206421; -.
DR PATRIC; fig|679202.3.peg.2505; -.
DR Proteomes; UP000005056; Unassembled WGS sequence.
DR GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR CDD; cd01164; FruK_PfkB_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR022463; 1-PFruKinase.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR017583; Tagatose/fructose_Pkinase.
DR NCBIfam; TIGR03168; 1-PFK; 1.
DR NCBIfam; TIGR03828; pfkB; 1.
DR PANTHER; PTHR46566:SF5; 1-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR46566; 1-PHOSPHOFRUCTOKINASE-RELATED; 1.
DR Pfam; PF00294; PfkB; 1.
DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU369061};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU369061};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU369061};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT DOMAIN 14..293
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 312 AA; 33756 MW; 067E5CF7C584FEA8 CRC64;
MSRRVATITL NPAYDLVGFC PEIERGEVNL VKTTGLHAAG KGINVAKVLK DLGIDVTVGG
FLGKDNQDGF QQLFSELGIA NRFQVVQGRT RINVKLTEKD GEVTDFNFSG FEVTPADWER
FVTDSLSWLG QFDMVCVSGS LPSGVSPEAF TDWMTRLRSQ CPCIIFDSSR EALVAGLKAA
PWLVKPNRRE LEIWAGRKLP EMKDVIEAAH ALREQGIAHV VISLGAEGAL WVNASGEWIA
KPPSVDVVST VGAGDSMVGG LIYGLLMRES SEHTLRLATA VAALAVSQSN VGITDRPQLA
AMMARVDLQP FN
//