LACC_STRPF
ID LACC_STRPF Reviewed; 309 AA.
AC Q1J4Q3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=MGAS10750_Spy1733;
OS Streptococcus pyogenes serotype M4 (strain MGAS10750).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=370554;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGAS10750;
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; CP000262; ABF38683.1; -; Genomic_DNA.
DR RefSeq; WP_011529002.1; NC_008024.1.
DR AlphaFoldDB; Q1J4Q3; -.
DR SMR; Q1J4Q3; -.
DR EnsemblBacteria; ABF38683; ABF38683; MGAS10750_Spy1733.
DR KEGG; spi:MGAS10750_Spy1733; -.
DR HOGENOM; CLU_050013_5_0_9; -.
DR OMA; GHVNMAH; -.
DR UniPathway; UPA00704; UER00715.
DR Proteomes; UP000002434; 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; 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.
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_1000068942"
SQ SEQUENCE 309 AA; 33504 MW; B5B004A5021E4FF1 CRC64;
MILTVTLNPA IDVSYPLDEL KCDTVNRVVD VTKTPGDKGL NVCRVLNDFG ETVKATGCIG
GESGDFIINH LPDSILSRFY KISGDTRTCI AILHEGNQTE ILEKGPLLSV EEIDGFTHHF
KYLLNDVDVV TLSGSLPAGM PDDYYQKLIG IANLNGKKTV LDCSGNALEA VLKGDSKPTV
IKPNLEELSQ LLGKEMTKDF EALKEVLQDE LFEGIEWIIV SLGADGVFAK HNDTFYNVDI
PKIEIVSAVG SGDSTVAGIA SGLANDEDDR ALLTKANVLG MLNAQEKTTG HVNMANYDKL
YQSIKVKEV