K1PF_BORBU
ID K1PF_BORBU Reviewed; 307 AA.
AC O51575;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=1-phosphofructokinase {ECO:0000250|UniProtKB:P0AEW9};
DE EC=2.7.1.56 {ECO:0000250|UniProtKB:P0AEW9};
DE AltName: Full=Fructose 1-phosphate kinase {ECO:0000250|UniProtKB:P0AEW9};
DE Short=Fru1PK {ECO:0000250|UniProtKB:P0AEW9};
GN Name=fruK; OrderedLocusNames=BB_0630;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-
CC phosphate to fructose-l,6-bisphosphate. {ECO:0000250|UniProtKB:P0AEW9}.
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:0000250|UniProtKB:P0AEW9};
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AE000783; AAC66983.1; -; Genomic_DNA.
DR PIR; E70178; E70178.
DR RefSeq; NP_212764.1; NC_001318.1.
DR RefSeq; WP_010889784.1; NC_001318.1.
DR AlphaFoldDB; O51575; -.
DR SMR; O51575; -.
DR STRING; 224326.BB_0630; -.
DR PRIDE; O51575; -.
DR DNASU; 1195481; -.
DR EnsemblBacteria; AAC66983; AAC66983; BB_0630.
DR KEGG; bbu:BB_0630; -.
DR PATRIC; fig|224326.49.peg.1020; -.
DR HOGENOM; CLU_050013_1_0_12; -.
DR OMA; QLNEPGP; -.
DR PHI-base; PHI:6527; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 Pfam; PF00294; PfkB; 1.
DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR03168; 1-PFK; 1.
DR TIGRFAMs; TIGR03828; pfkB; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..307
FT /note="1-phosphofructokinase"
FT /id="PRO_0000080075"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 217..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 249..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
SQ SEQUENCE 307 AA; 33595 MW; 94DF27BD61246D39 CRC64;
MIYTLTLNPS VDYKIVLKEF QEESLNYALN NNFFAGGKGI NVSTVLKNLG KPSTALGFLG
GFTGDYIRFS LDSRGIKNDF IKIKYDTRLN IKMIANGRET EINANSPDIS ENEFELLKNK
LKNLANNSTL VMSGSVPAAL GEDAYNEIAN SISNDVKLII DTSGKPLRKI LRLNPFLIKP
NIYELEDLFN AKFDSTKELI KIGKNLVESG VQNIIISMGS DGAIFIGGKN VAFRAFVPKI
NFVSTIGAGD SVIAGFVYAF DNGSTLEDSF KFGVAAGTAT ALKGNLCEFQ DVKKMLCQIR
VEDIYTS