COAX_LEGPH
ID COAX_LEGPH Reviewed; 256 AA.
AC Q5ZX22;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Type III pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_01274};
DE EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_01274};
DE AltName: Full=PanK-III {ECO:0000255|HAMAP-Rule:MF_01274};
DE AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_01274};
GN Name=coaX {ECO:0000255|HAMAP-Rule:MF_01274}; OrderedLocusNames=lpg0911;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP +
CC H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC EC=2.7.1.33; Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC -!- COFACTOR:
CC Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC Note=A monovalent cation. Ammonium or potassium. {ECO:0000255|HAMAP-
CC Rule:MF_01274};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01274}.
CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01274}.
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DR EMBL; AE017354; AAU26998.1; -; Genomic_DNA.
DR RefSeq; WP_010946646.1; NC_002942.5.
DR RefSeq; YP_094945.1; NC_002942.5.
DR PDB; 3DJC; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=2-256.
DR PDBsum; 3DJC; -.
DR AlphaFoldDB; Q5ZX22; -.
DR SMR; Q5ZX22; -.
DR STRING; 272624.lpg0911; -.
DR PaxDb; Q5ZX22; -.
DR EnsemblBacteria; AAU26998; AAU26998; lpg0911.
DR GeneID; 66490093; -.
DR KEGG; lpn:lpg0911; -.
DR PATRIC; fig|272624.6.peg.944; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_1_0_6; -.
DR OMA; HEPWLTL; -.
DR UniPathway; UPA00241; UER00352.
DR EvolutionaryTrace; Q5ZX22; -.
DR Proteomes; UP000000609; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004619; Type_III_PanK.
DR PANTHER; PTHR34265; PTHR34265; 1.
DR Pfam; PF03309; Pan_kinase; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00671; baf; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Metal-binding; Nucleotide-binding; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..256
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000267553"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 106..109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 129
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:3DJC"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:3DJC"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:3DJC"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:3DJC"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3DJC"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3DJC"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3DJC"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:3DJC"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3DJC"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3DJC"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:3DJC"
FT STRAND 123..139
FT /evidence="ECO:0007829|PDB:3DJC"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:3DJC"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:3DJC"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3DJC"
FT HELIX 184..210
FT /evidence="ECO:0007829|PDB:3DJC"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:3DJC"
FT STRAND 217..223
FT /evidence="ECO:0007829|PDB:3DJC"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:3DJC"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:3DJC"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:3DJC"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:3DJC"
SQ SEQUENCE 256 AA; 27744 MW; 1D9D254FBD6180A4 CRC64;
MILCIDVGNS HIYGGVFDGD EIKLRFRHTS KVSTSDELGI FLKSVLRENN CSPETIRKIA
ICSVVPQVDY SLRSACVKYF SIDPFLLQAG VKTGLNIKYR NPVEVGADRI ANAIAATHSF
PNQNIIVIDF GTATTFCAIS HKKAYLGGAI LPGLRLSADA LSKNTAKLPS VEIIKTESVV
GRSTIESIQS GVYYGVLGAC KELIQRIHHE AFNGDQILIL ATGGFASLFD KQGLYDHLVP
DLVLQGIRLA AMMNTA
