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Entry: A7MLK9_CROS8
LinkDB: A7MLK9_CROS8
Original site: A7MLK9_CROS8 
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
//
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