ID I6L928_STRMU Unreviewed; 303 AA.
AC I6L928; Q1LZ60;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Tagatose-6-phosphate kinase {ECO:0000256|PIRNR:PIRNR000535};
DE EC=2.7.1.144 {ECO:0000256|PIRNR:PIRNR000535};
GN Name=pfkB {ECO:0000313|EMBL:AAN58586.1};
GN Synonyms=fruK {ECO:0000313|EMBL:DAA01813.1};
GN OrderedLocusNames=SMU_871 {ECO:0000313|EMBL:AAN58586.1};
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN58586.1, ECO:0000313|Proteomes:UP000002512};
RN [1] {ECO:0000313|EMBL:DAA01813.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UA159 {ECO:0000313|EMBL:DAA01813.1};
RX PubMed=11750824; DOI=10.1111/j.1574-6968.2001.tb10969.x;
RA Wen Z.T., Browngardt C., Burne R.A.;
RT "Characterization of two operons that encode components of fructose-
RT specific enzyme II of the sugar:phosphotransferase system of Streptococcus
RT mutans.";
RL FEMS Microbiol. Lett. 205:337-342(2001).
RN [2] {ECO:0000313|EMBL:AAN58586.1, ECO:0000313|Proteomes:UP000002512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512}, and
RC UA159 {ECO:0000313|EMBL:AAN58586.1};
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [3] {ECO:0000313|EMBL:AAN58586.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UA159 {ECO:0000313|EMBL:AAN58586.1};
RA Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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 + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose
CC 1,6-bisphosphate + H(+); Xref=Rhea:RHEA:12420, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58694, ChEBI:CHEBI:58695,
CC ChEBI:CHEBI:456216; EC=2.7.1.144;
CC Evidence={ECO:0000256|PIRNR:PIRNR000535};
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 -!- PATHWAY: Carbohydrate metabolism; D-tagatose 6-phosphate degradation;
CC D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-
CC phosphate: step 1/2. {ECO:0000256|PIRNR:PIRNR000535}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. LacC
CC subfamily. {ECO:0000256|PIRNR:PIRNR000535}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC {ECO:0000256|ARBA:ARBA00005380}.
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DR EMBL; AE014133; AAN58586.1; -; Genomic_DNA.
DR EMBL; BK000031; DAA01813.1; -; Genomic_DNA.
DR RefSeq; NP_721280.1; NC_004350.2.
DR RefSeq; WP_002262019.1; NC_004350.2.
DR AlphaFoldDB; I6L928; -.
DR STRING; 210007.SMU_871; -.
DR GeneID; 66817694; -.
DR KEGG; smu:SMU_871; -.
DR PATRIC; fig|210007.7.peg.777; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_1_0_9; -.
DR OrthoDB; 9801219at2; -.
DR UniPathway; UPA00704; UER00715.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009024; F:tagatose-6-phosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0005988; P:lactose metabolic process; IEA:UniProtKB-KW.
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:SF1; 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|PIRNR:PIRNR000535};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU369061};
KW Lactose metabolism {ECO:0000256|PIRNR:PIRNR000535};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000535};
KW Reference proteome {ECO:0000313|Proteomes:UP000002512};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT DOMAIN 22..280
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 303 AA; 32803 MW; EA67915FAE32626E CRC64;
MIYTVTLNPS IDFIVRIDSV KIGSVNRMDS DDKFVGGKGI NVSRILKRLG QDNTATGFIG
GFTGRFVEEG LIAEGIKTNF VHVNQDTRIN VKIKADQETE INGTGPVITK EQVLALENIL
QQLSQDDTVV FAGSAPSNLG NQIYERLIPL VRQTGAQIVC DFEGQTLLDA LDYQPLLVKP
NNHELEAIFK VNLNGITDVE KYARQILAKG AQNVIISMAG DGALLVTSDA TYFAKPIKGQ
VRNSVGAGDS MVAGFTGEFV KSANPLEALK WGVACGTATA FSDDLASIDF IKETYEKVEV
EKL
//
