K1PF_BACSU
ID K1PF_BACSU Reviewed; 303 AA.
AC O31714;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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; Synonyms=fruB; OrderedLocusNames=BSU14390;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Caldwell R.M., Ferrari E.;
RT "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(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; AF012285; AAC24914.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13312.1; -; Genomic_DNA.
DR PIR; A69627; A69627.
DR RefSeq; NP_389322.1; NC_000964.3.
DR RefSeq; WP_003244923.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31714; -.
DR SMR; O31714; -.
DR STRING; 224308.BSU14390; -.
DR jPOST; O31714; -.
DR PaxDb; O31714; -.
DR PRIDE; O31714; -.
DR EnsemblBacteria; CAB13312; CAB13312; BSU_14390.
DR GeneID; 938761; -.
DR KEGG; bsu:BSU14390; -.
DR PATRIC; fig|224308.179.peg.1569; -.
DR eggNOG; COG1105; Bacteria.
DR InParanoid; O31714; -.
DR OMA; GETRSNI; -.
DR PhylomeDB; O31714; -.
DR BioCyc; BSUB:BSU14390-MON; -.
DR Proteomes; UP000001570; 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; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..303
FT /note="1-phosphofructokinase"
FT /id="PRO_0000080074"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 248..249
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
SQ SEQUENCE 303 AA; 32791 MW; DA33D3BEA1638F30 CRC64;
MIYTVTLNPS VDYIVHVEDF TVGGLNRSSY DTKYPGGKGI NVSRLLKRHH VASKALGFVG
GFTGEYIKTF LREENLETAF SEVKGDTRIN VKLKTGDETE INGQGPTISD EDFKAFLEQF
QSLQEGDIVV LAGSIPSSLP HDTYEKIAEA CKQQNARVVL DISGEALLKA TEMKPFLMKP
NHHELGEMFG TAITSVEEAV PYGKKLVEQG AEHVIVSMAG DGALLFTNEA VYFANVPKGK
LVNSVGAGDS VVAGFLAGIS KQLPLEEAFR LGVTSGSATA FSEELGTEEF VQQLLPEVKV
TRL
