LACC_STRMU
ID LACC_STRMU Reviewed; 310 AA.
AC P26421;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tagatose-6-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_01557};
DE EC=2.7.1.144 {ECO:0000255|HAMAP-Rule:MF_01557};
DE AltName: Full=Phosphotagatokinase {ECO:0000255|HAMAP-Rule:MF_01557};
GN Name=lacC {ECO:0000255|HAMAP-Rule:MF_01557}; OrderedLocusNames=SMU_1494;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400164; DOI=10.1128/jb.174.19.6159-6170.1992;
RA Rosey E.L., Stewart G.C.;
RT "Nucleotide and deduced amino acid sequences of the lacR, lacABCD, and
RT lacFE genes encoding the repressor, tagatose 6-phosphate gene cluster, and
RT sugar-specific phosphotransferase system components of the lactose operon
RT of Streptococcus mutans.";
RL J. Bacteriol. 174:6159-6170(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., 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).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01557};
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:0000255|HAMAP-Rule:MF_01557}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. LacC
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01557}.
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DR EMBL; M80797; AAA26906.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59148.1; -; Genomic_DNA.
DR PIR; E43258; E43258.
DR RefSeq; NP_721842.1; NC_004350.2.
DR RefSeq; WP_002262465.1; NC_004350.2.
DR AlphaFoldDB; P26421; -.
DR SMR; P26421; -.
DR STRING; 210007.SMU_1494; -.
DR PRIDE; P26421; -.
DR EnsemblBacteria; AAN59148; AAN59148; SMU_1494.
DR GeneID; 66819106; -.
DR KEGG; smu:SMU_1494; -.
DR PATRIC; fig|210007.7.peg.1330; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_5_0_9; -.
DR OMA; QLNEPGP; -.
DR PhylomeDB; P26421; -.
DR UniPathway; UPA00704; UER00715.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009024; F:tagatose-6-phosphate kinase activity; ISA:CACAO.
DR GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019512; P:lactose catabolic process via tagatose-6-phosphate; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd01164; FruK_PfkB_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_01557; LacC; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR005926; LacC.
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; TIGR01231; lacC; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Lactose metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..310
FT /note="Tagatose-6-phosphate kinase"
FT /id="PRO_0000203930"
SQ SEQUENCE 310 AA; 33363 MW; 3A77E913FC7B0D4E CRC64;
MMLTVTMNPS IDIAYQLDDL KVDTVNRVIE THKTPGGKGL NVTRVLSQLG DDVLASGLLG
GKLGEFLEAE LDKSAIKHSF YKISAETRNC IAILHGGYQT EILEQGPYVS AKESKGFLEF
FEKLLPKLEV VAISGSLPKG VPVDYYSQMI AICKQHQVPI VLDCSGQALL EVLNGAAKPT
VIKPNTEELS QIMEREITND VAVLKHALAS PIFSGIDWII VSLGSQGAFA KHGQTFYKVT
IPKIAVVNPV GSGDSTVAGI TSALAAGASD EKLLKKANTL GMLNAQEKLT GHVNLENYDN
LYQQIEVAEV