COAX_BURCJ
ID COAX_BURCJ Reviewed; 266 AA.
AC B4E9P3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
GN OrderedLocusNames=BceJ2315_06870; ORFNames=BCAL0693;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR51002.1; -; Genomic_DNA.
DR RefSeq; WP_006482096.1; NC_011000.1.
DR PDB; 5B8H; X-ray; 2.20 A; A/B=1-266.
DR PDBsum; 5B8H; -.
DR AlphaFoldDB; B4E9P3; -.
DR SMR; B4E9P3; -.
DR STRING; 216591.BCAL0693; -.
DR EnsemblBacteria; CAR51002; CAR51002; BCAL0693.
DR KEGG; bcj:BCAL0693; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_0_0_4; -.
DR OMA; NSFIKWR; -.
DR OrthoDB; 2039419at2; -.
DR BioCyc; BCEN216591:G1G1V-784-MON; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000001035; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 Nucleotide-binding; Potassium; Transferase.
FT CHAIN 1..266
FT /note="Type III pantothenate kinase"
FT /id="PRO_1000140227"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 103..106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:5B8H"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 121..136
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 189..216
FT /evidence="ECO:0007829|PDB:5B8H"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 229..235
FT /evidence="ECO:0007829|PDB:5B8H"
FT HELIX 246..256
FT /evidence="ECO:0007829|PDB:5B8H"
SQ SEQUENCE 266 AA; 27786 MW; 4915280AF7E1878A CRC64;
MSEPHLLIDA GNSRIKWALA DARRTLVDTG AFGHTRDGGA DPDWSRLPRP RGAWISNVAG
ADVAARIDAL LDARWPGLPR TTIRSRPAQC GVTNGYTTPE QLGSDRWAGL IGAHAAFPGE
HLLIATFGTA TTLEALRADG CFTGGLIAPG WALMMRALGT HTAQLPTLTT DIASGLLAGA
QAEPFQVDTP RSLSAGCLYA QAGLIERAWR DLVAAWQAPV RLVLAGGAAD DVARALTIAH
TRHDTLILSG LALIAADAAD PATAPD
