K1PF_VIBCH
ID K1PF_VIBCH Reviewed; 317 AA.
AC Q9KM71;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 {ECO:0000303|PubMed:33476373};
GN OrderedLocusNames=VC_A0517 {ECO:0000312|EMBL:AAF96420.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=33476373; DOI=10.1093/nar/gkab013;
RA Yoon C.K., Kang D., Kim M.K., Seok Y.J.;
RT "Vibrio cholerae FruR facilitates binding of RNA polymerase to the fru
RT promoter in the presence of fructose 1-phosphate.";
RL Nucleic Acids Res. 49:1397-1410(2021).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=33649152; DOI=10.1128/jb.00044-21;
RA Beck C., Perry S., Stoebel D.M., Liu J.M.;
RT "Cra and cAMP receptor protein have opposing roles in the regulation of
RT fruB in Vibrio cholerae.";
RL J. Bacteriol. 203:0-0(2021).
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 -!- INDUCTION: Part of the fruBKA (fru) operon, which is induced in the
CC presence of fructose via the FruR (Cra) regulatory protein
CC (PubMed:33476373). Transcription is repressed by FruR in the absence of
CC fructose (PubMed:33649152). CRP activates expression of the fru operon
CC in the absence of glucose (PubMed:33649152). The two regulators can
CC work independently to control the expression of the operon depending on
CC carbon source availability (PubMed:33649152).
CC {ECO:0000269|PubMed:33476373, ECO:0000269|PubMed:33649152}.
CC -!- DISRUPTION PHENOTYPE: Does not affect growth on glucose. Mutant shows a
CC severe growth defect on fructose. {ECO:0000269|PubMed:33476373}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; AE003853; AAF96420.1; -; Genomic_DNA.
DR PIR; C82450; C82450.
DR RefSeq; NP_232908.1; NC_002506.1.
DR RefSeq; WP_000163391.1; NZ_LT906615.1.
DR SMR; Q9KM71; -.
DR STRING; 243277.VC_A0517; -.
DR PRIDE; Q9KM71; -.
DR DNASU; 2612820; -.
DR EnsemblBacteria; AAF96420; AAF96420; VC_A0517.
DR GeneID; 57741921; -.
DR KEGG; vch:VC_A0517; -.
DR PATRIC; fig|243277.26.peg.3143; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_0_1_6; -.
DR OMA; GETRSNI; -.
DR BioCyc; VCHO:VCA0517-MON; -.
DR Proteomes; UP000000584; Chromosome 2.
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.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..317
FT /note="1-phosphofructokinase"
FT /id="PRO_0000453371"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 223..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
FT BINDING 254..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A9J6"
SQ SEQUENCE 317 AA; 34192 MW; 6A0B65C3713AA033 CRC64;
MTKKVVTITL NPALDLTGSV NQLNVGSVSL VGQSSLHAAG KGVNVAKVLS ELGAQVTVTG
FLGRDNQELF CQLFEQLGVQ DAFIRIAGAT RINVKLVEQS GAVSDINFPG IQVTEADIEA
FEATLQRLAQ DHDYFVLAGS LPQGISPQRC AGWIAQLRSM NKKVLFDSSR DALLAGLDAK
PWLIKPNDEE LSQWCGRELT TLTDCQQAAA ELAQKQIENI VISMGAEGVM WLHENQWLHA
KPPKMQVVST VGAGDTLVAG LCWGHMQRME KESLLRFATA LSALAVTQVG VGLGDREQLN
TLQQQIQVSA LYPTMGA
