COAX_BORPE
ID COAX_BORPE Reviewed; 267 AA.
AC Q45338; Q45373;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Type III pantothenate kinase;
DE EC=2.7.1.33;
DE AltName: Full=Bvg accessory factor;
DE AltName: Full=PanK-III;
DE AltName: Full=Pantothenic acid kinase;
GN Name=coaX; Synonyms=baf; OrderedLocusNames=BP0097;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BP504;
RX PubMed=7601846; DOI=10.1128/jb.177.13.3801-3807.1995;
RA Deshazer D., Wood G.E., Friedman R.L.;
RT "Identification of a Bordetella pertussis regulatory factor required for
RT transcription of the pertussis toxin operon in Escherichia coli.";
RL J. Bacteriol. 177:3801-3807(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38.
RC STRAIN=BP504;
RA Wood G.E., Friedman R.L.;
RT "Identification of a birA homolog in Bordetella pertussis.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 239-267.
RC STRAIN=BP536;
RX PubMed=8821935; DOI=10.1046/j.1365-2958.1996.354877.x;
RA Allen A.G., Maskell D.J.;
RT "The identification, cloning and mutagenesis of a genetic locus required
RT for lipopolysaccharide biosynthesis in Bordetella pertussis.";
RL Mol. Microbiol. 19:37-52(1996).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000250}.
CC -!- FUNCTION: Activates transcription of the pertussis toxin operon in a
CC BvgAS-dependent manner. May interact with the alpha subunit of RNA
CC polymerase.
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;
CC -!- COFACTOR:
CC Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000250};
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC Note=A monovalent cation. Ammonium or potassium. {ECO:0000250};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC {ECO:0000305}.
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DR EMBL; U12020; AAA75361.1; -; Genomic_DNA.
DR EMBL; BX640411; CAE40475.1; -; Genomic_DNA.
DR EMBL; AF016461; AAC68834.1; -; Genomic_DNA.
DR EMBL; X90711; CAA62242.1; -; Genomic_DNA.
DR PIR; I40327; I40327.
DR RefSeq; NP_878999.1; NC_002929.2.
DR RefSeq; WP_010929617.1; NZ_CP039022.1.
DR AlphaFoldDB; Q45338; -.
DR SMR; Q45338; -.
DR STRING; 257313.BP0097; -.
DR GeneID; 45387503; -.
DR KEGG; bpe:BP0097; -.
DR PATRIC; fig|257313.5.peg.96; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_0_0_4; -.
DR OMA; TCITYDF; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000002676; Chromosome.
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.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Potassium; Reference proteome; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..267
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000064809"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 103..106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 181
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 267 AA; 27845 MW; 336A615F67B57901 CRC64;
MIILIDSGNS RLKVGWFDPD APQAAREPAP VAFDNLDLDA LGRWLATLPR RPQRALGVNV
AGLARGEAIA ATLRAGGCDI RWLRAQPLAM GLRNGYRNPD QLGADRWACM VGVLARQPSV
HPPLLVASFG TATTLDTIGP DNVFPGGLIL PGPAMMRGAL AYGTAHLPLA DGLVADYPID
THQAIASGIA AAQAGAIVRQ WLAGRQRYGQ APEIYVAGGG WPEVRQEAER LLAVTGAAFG
ATPQPTYLDS PVLDGLAALA AQGAPTA
