K1PF_XANCP
ID K1PF_XANCP Reviewed; 318 AA.
AC P23354;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=1-phosphofructokinase {ECO:0000303|PubMed:1655739};
DE EC=2.7.1.56 {ECO:0000269|PubMed:1655739};
DE AltName: Full=Fructose 1-phosphate kinase {ECO:0000303|PubMed:1655739};
DE Short=Fru1PK {ECO:0000250|UniProtKB:P0AEW9};
GN Name=fruK {ECO:0000303|PubMed:1655739}; OrderedLocusNames=XCC2371;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INDUCTION.
RC STRAIN=ATCC 13951 / NCIB 11803 / NRRL B-1459;
RX PubMed=1655739; DOI=10.1016/s0021-9258(18)55249-2;
RA de Crecy-Lagard V., Bouvet O.M., Lejeune P., Danchin A.;
RT "Fructose catabolism in Xanthomonas campestris pv. campestris. Sequence of
RT the PTS operon, characterization of the fructose-specific enzymes.";
RL J. Biol. Chem. 266:18154-18161(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-
CC phosphate to fructose-l,6-bisphosphate. {ECO:0000269|PubMed:1655739}.
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:0000269|PubMed:1655739};
CC -!- INDUCTION: Induced by fructose. {ECO:0000269|PubMed:1655739}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; M69242; AAA27601.1; -; Genomic_DNA.
DR EMBL; AE008922; AAM41649.1; -; Genomic_DNA.
DR PIR; A40944; A40944.
DR RefSeq; NP_637725.1; NC_003902.1.
DR RefSeq; WP_011037514.1; NC_003902.1.
DR AlphaFoldDB; P23354; -.
DR SMR; P23354; -.
DR STRING; 340.xcc-b100_1801; -.
DR EnsemblBacteria; AAM41649; AAM41649; XCC2371.
DR KEGG; xcc:XCC2371; -.
DR PATRIC; fig|190485.4.peg.2525; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_0_1_6; -.
DR OMA; GETRSNI; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008662; F:1-phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008443; F:phosphofructokinase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..318
FT /note="1-phosphofructokinase"
FT /id="PRO_0000080082"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 228..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 259..260
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT CONFLICT 14
FT /note="I -> T (in Ref. 1; AAA27601)"
FT /evidence="ECO:0000305"
FT CONFLICT 80..81
FT /note="TD -> GN (in Ref. 1; AAA27601)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..174
FT /note="ARVLLDTSGAPL -> STRPARHQRCAA (in Ref. 1; AAA27601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 32592 MW; 5B7EC573D1B790A0 CRC64;
MSLQAITVTL NPAIDQTIQL DRLQPGAVHR ASSVRNDAGG KGINVAACLA DWGSQVAALG
VLGVGNAGVF EALFRERGIT DHCHRVAGDT RTNLKLVEAQ VNETTDINLP GLQLGQAHLQ
GVADHLAPLL RAGLPVVLSG SLPAGLPEDS WAQLQAQASA AGARVLLDTS GAPLVAALAA
APVAMPYAVK PNRHELEAWT GHPLGDHAAL TAAAHALIAR GIQLVVISMG TEGALFVQRD
QQLIARPPRL AQGSSVGAGD AMVAGLAAAL LDDATELEQC ARLATAFSMC RLESGDARRI
TPEGVRDAAA AVVIGAVP
