LACC_STRPD
ID LACC_STRPD Reviewed; 309 AA.
AC Q1JEY9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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};
GN OrderedLocusNames=MGAS10270_Spy1705;
OS Streptococcus pyogenes serotype M2 (strain MGAS10270).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370552;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10270;
RX PubMed=16636287; DOI=10.1073/pnas.0510279103;
RA Beres S.B., Richter E.W., Nagiec M.J., Sumby P., Porcella S.F., DeLeo F.R.,
RA Musser J.M.;
RT "Molecular genetic anatomy of inter- and intraserotype variation in the
RT human bacterial pathogen group A Streptococcus.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7059-7064(2006).
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; CP000260; ABF34770.1; -; Genomic_DNA.
DR RefSeq; WP_020905488.1; NC_008022.1.
DR AlphaFoldDB; Q1JEY9; -.
DR SMR; Q1JEY9; -.
DR EnsemblBacteria; ABF34770; ABF34770; MGAS10270_Spy1705.
DR KEGG; sph:MGAS10270_Spy1705; -.
DR HOGENOM; CLU_050013_5_0_9; -.
DR OMA; GHVNMAH; -.
DR UniPathway; UPA00704; UER00715.
DR Proteomes; UP000002436; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009024; F:tagatose-6-phosphate kinase activity; IEA:UniProtKB-UniRule.
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.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Lactose metabolism; Nucleotide-binding; Transferase.
FT CHAIN 1..309
FT /note="Tagatose-6-phosphate kinase"
FT /id="PRO_1000068941"
SQ SEQUENCE 309 AA; 33513 MW; 32404A954BE87A6D CRC64;
MILTVTLNPA IDVSYPLNEL KCDTVNRVVD VTKTPGGKGL NVSRVLNDFG ETVKATGCIG
GESGDFIINH LPDSILSRFY KISGDTRTCI AILHEGNQTE ILEKGPLLSV DEIDGFTHHF
KYLLNDVDVV TLSGSLPAGM PDDYYQKLIK IANLNGKKTV LDCSGNALEA VLKGDSKPTV
IKPNLEELSQ LLGKEMTKDF EALKEVLQDE LFEGIEWIIV SLGADGVFAK HKDTFYNVDI
PKIKIVSAVG SGDSTVAGIA SGLANDEDDR ALLTKANVLG MLNAQEKTTG HVNMANYDKL
YQSIKIKEV