ID D4CT66_9FUSO Unreviewed; 352 AA.
AC D4CT66;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=1-phosphofructokinase {ECO:0000256|ARBA:ARBA00013596, ECO:0000256|RuleBase:RU369061};
DE Short=Fru1PK {ECO:0000256|RuleBase:RU369061};
DE EC=2.7.1.56 {ECO:0000256|ARBA:ARBA00012131, ECO:0000256|RuleBase:RU369061};
DE AltName: Full=Fructose 1-phosphate kinase {ECO:0000256|ARBA:ARBA00032802, ECO:0000256|RuleBase:RU369061};
GN Name=pfkB {ECO:0000313|EMBL:EFE87436.1};
GN ORFNames=FUSPEROL_00578 {ECO:0000313|EMBL:EFE87436.1};
OS Fusobacterium periodonticum ATCC 33693.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=546275 {ECO:0000313|EMBL:EFE87436.1, ECO:0000313|Proteomes:UP000003748};
RN [1] {ECO:0000313|EMBL:EFE87436.1, ECO:0000313|Proteomes:UP000003748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33693 {ECO:0000313|EMBL:EFE87436.1,
RC ECO:0000313|Proteomes:UP000003748};
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., Nelson J., Hou S., 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 (FEB-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|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:EFE87436.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACJY01000037; EFE87436.1; -; Genomic_DNA.
DR AlphaFoldDB; D4CT66; -.
DR STRING; 546275.FUSPEROL_00578; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_1_0_0; -.
DR Proteomes; UP000003748; 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:SF1; 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; 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 54..324
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 352 AA; 39628 MW; 2CD6D69C25A3887F CRC64;
MSACLKPTCW QVLPNLQRIL DFYTLRNLAS NELFSYLILK GELMIYSVTL NPSIDFIVRV
KDFQIGETNR AYEDNFFAGG KGIMVSKLLK NVGTECVNLG FLGGFTGAFI EENLKKLNIP
SDFVSVEENT RINVKLKTEE ETEINCQGPK ISEKEKEEFL DKIRKIKSDD FVILSGSVPS
NLGNDFYINI IEILNENSVK FTLDSSGETF KKSLKYKPFL IKPNKDELKE YAKREFKDNK
EIIDYVRTNL VGMAENVIIS LGGEGALYIA KDFSLFAQPF KAKESVVNTV GAGDSVVAGF
VNYMLKENDV KKAFRFAVAC GTATSFSEDI GELDFIEEIS KKLVIEKEHY GN
//
