ID A7MLK9_CROS8 Unreviewed; 312 AA.
AC A7MLK9;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 24-JAN-2024, entry version 101.
DE RecName: Full=Phosphofructokinase {ECO:0000256|PIRNR:PIRNR000535};
GN OrderedLocusNames=ESA_01075 {ECO:0000313|EMBL:ABU76343.1};
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU76343.1, ECO:0000313|Proteomes:UP000000260};
RN [1] {ECO:0000313|EMBL:ABU76343.1, ECO:0000313|Proteomes:UP000000260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU76343.1,
RC ECO:0000313|Proteomes:UP000000260};
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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|PIRNR:PIRNR000535,
CC ECO:0000256|RuleBase:RU369061}.
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DR EMBL; CP000783; ABU76343.1; -; Genomic_DNA.
DR RefSeq; WP_004387452.1; NC_009778.1.
DR AlphaFoldDB; A7MLK9; -.
DR GeneID; 56729944; -.
DR KEGG; esa:ESA_01075; -.
DR HOGENOM; CLU_050013_0_1_6; -.
DR OMA; AGMVHGL; -.
DR Proteomes; UP000000260; Chromosome.
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:SF5; 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; PS00583; PFKB_KINASES_1; 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 Reference proteome {ECO:0000313|Proteomes:UP000000260};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT DOMAIN 14..293
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 312 AA; 33780 MW; 3CD1824ED5A25320 CRC64;
MSRRVATITL NPAYDLVGYC AEIERGEVNL VRTTGLHAAG KGINVAKVLK DLGIDVTVGG
FLGKDNQDGF QQLFSELGIA NRFQVVQGRT RINVKLTEKD GEVTDLNFSG FEVTPADWER
FVNDSLTWLG QFDMVCVSGS LPSGVSPEAF TDWMTRLRSQ CPCIIFDSSR EALVAGLKAA
PWLVKPNRRE LEIWAGRKLP ELKDVIEAAH ALREQGIAHV VISLGAEGAL WVNASGEWIA
KPPSCDVVST VGAGDSMVGG LIYGLLMRES SEHTLRLATA VAALAVSQSN VGITDRTQLA
AMMARVDLKP FH
//