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Database: UniProt
Entry: E6BKB1_ECOLX
LinkDB: E6BKB1_ECOLX
Original site: E6BKB1_ECOLX 
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
//
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