LACC_CLOPE
ID LACC_CLOPE Reviewed; 310 AA.
AC Q8XNK5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=CPE0328;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(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; BA000016; BAB80034.1; -; Genomic_DNA.
DR RefSeq; WP_011009744.1; NC_003366.1.
DR AlphaFoldDB; Q8XNK5; -.
DR SMR; Q8XNK5; -.
DR STRING; 195102.gene:10489584; -.
DR EnsemblBacteria; BAB80034; BAB80034; BAB80034.
DR KEGG; cpe:CPE0328; -.
DR HOGENOM; CLU_050013_5_0_9; -.
DR OMA; QLNEPGP; -.
DR UniPathway; UPA00704; UER00715.
DR Proteomes; UP000000818; 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; 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_0000203913"
SQ SEQUENCE 310 AA; 34049 MW; 0AC98BA5B8CA6932 CRC64;
MILTITMNPS IDISYPLDVL NLDSVNRVTK VTKTAGGKGL NVTRVLKQLD ADVLASGLLG
GFFGDFIKND LNINGIKHSF SDISGETRNC IAILHEGNQT EILESGPNIS EKEANNFLRH
FELLVDKANI ISISGSLPLG ISKDFYVKML SICNKKDKRV VLDCSGEELR QVLKNDSKPF
AIKPNIDELS DLLGVKVKDS IEDLKLILNT PMFNGIEWIV ISMGAKGSFA KHNDKFYRVI
IPKIQVVNPV GSGDSTIAGL TKGLNDGETD ENVLKIANTL GMLNAQEHIT GYVNMDNYKN
LFEKIKVVEV