COAX_CAMJE
ID COAX_CAMJE Reviewed; 209 AA.
AC Q0PBB6;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Cj0394c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL111168; CAL34544.1; -; Genomic_DNA.
DR PIR; H81382; H81382.
DR RefSeq; WP_002864777.1; NC_002163.1.
DR RefSeq; YP_002343831.1; NC_002163.1.
DR PDB; 2NRH; X-ray; 2.30 A; A/B=2-209.
DR PDBsum; 2NRH; -.
DR AlphaFoldDB; Q0PBB6; -.
DR SMR; Q0PBB6; -.
DR IntAct; Q0PBB6; 7.
DR STRING; 192222.Cj0394c; -.
DR PaxDb; Q0PBB6; -.
DR PRIDE; Q0PBB6; -.
DR EnsemblBacteria; CAL34544; CAL34544; Cj0394c.
DR GeneID; 904717; -.
DR KEGG; cje:Cj0394c; -.
DR PATRIC; fig|192222.6.peg.385; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_1213471_0_0_7; -.
DR OMA; FHLETDY; -.
DR UniPathway; UPA00241; UER00352.
DR EvolutionaryTrace; Q0PBB6; -.
DR Proteomes; UP000000799; 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..209
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000267504"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 5..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 68
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 72..75
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 89
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2NRH"
FT STRAND 8..14
FT /evidence="ECO:0007829|PDB:2NRH"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:2NRH"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 73..79
FT /evidence="ECO:0007829|PDB:2NRH"
FT STRAND 83..100
FT /evidence="ECO:0007829|PDB:2NRH"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:2NRH"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 144..163
FT /evidence="ECO:0007829|PDB:2NRH"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:2NRH"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 176..180
FT /evidence="ECO:0007829|PDB:2NRH"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:2NRH"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:2NRH"
SQ SEQUENCE 209 AA; 23936 MW; C49313AA9E3D2D19 CRC64;
MLLCDIGNSN ANFLDDNKYF TLNIDQFLEF KNEQKIFYIN VNEHLKEHLK NQKNFINLEP
YFLFDTIYQG LGIDRIAACY TIEDGVVVDA GSAITIDIIS NSIHLGGFIL PGIANYKKIY
SHISPRLKSE FNTQVSLDAF PQKTMDALSY GVFKGIYLLI KDAAQNKKLY FTGGDGQFLA
NYFDHAIYDK LLIFRGMKKI IKENPNLLY
