LACC_ENTFA
ID LACC_ENTFA Reviewed; 313 AA.
AC Q833W9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=EF_1806;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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; AE016830; AAO81574.1; -; Genomic_DNA.
DR RefSeq; NP_815504.1; NC_004668.1.
DR RefSeq; WP_010706669.1; NZ_KE136528.1.
DR PDB; 2AWD; X-ray; 2.00 A; A/B=2-313.
DR PDB; 2F02; X-ray; 1.90 A; A/B=2-313.
DR PDBsum; 2AWD; -.
DR PDBsum; 2F02; -.
DR AlphaFoldDB; Q833W9; -.
DR SMR; Q833W9; -.
DR STRING; 226185.EF_1806; -.
DR DNASU; 1200692; -.
DR EnsemblBacteria; AAO81574; AAO81574; EF_1806.
DR KEGG; efa:EF1806; -.
DR PATRIC; fig|226185.45.peg.1712; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_5_0_9; -.
DR OMA; GHVNMAH; -.
DR UniPathway; UPA00704; UER00715.
DR EvolutionaryTrace; Q833W9; -.
DR Proteomes; UP000001415; 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 PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Lactose metabolism; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..313
FT /note="Tagatose-6-phosphate kinase"
FT /id="PRO_0000203914"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 61..73
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 271..287
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:2F02"
FT HELIX 296..303
FT /evidence="ECO:0007829|PDB:2F02"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:2F02"
SQ SEQUENCE 313 AA; 33817 MW; 90029311154D7BD2 CRC64;
MIVTVTMNPS IDISYLLDHL KLDTVNRTSQ VTKTPGGKGL NVTRVIHDLG GDVIATGVLG
GFHGAFIANE LKKANIPQAF TSIKEETRDS IAILHEGNQT EILEAGPTVS PEEISNFLEN
FDQLIKQAEI VTISGSLAKG LPSDFYQELV QKAHAQEVKV LLDTSGDSLR QVLQGPWKPY
LIKPNLEELE GLLGQDFSEN PLAAVQTALT KPMFAGIEWI VISLGKDGAI AKHHDQFYRV
KIPTIQAKNP VGSGDATIAG LAYGLAKDAP AAELLKWGMA AGMANAQERM TGHVDVENVK
KHLMNIQVVE IAK
