COAX_ACISJ
ID COAX_ACISJ Reviewed; 258 AA.
AC A1W3F9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Ajs_0534;
OS Acidovorax sp. (strain JS42).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax; unclassified Acidovorax.
OX NCBI_TaxID=232721;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS42;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000539; ABM40784.1; -; Genomic_DNA.
DR RefSeq; WP_011803993.1; NC_008782.1.
DR AlphaFoldDB; A1W3F9; -.
DR SMR; A1W3F9; -.
DR STRING; 232721.Ajs_0534; -.
DR EnsemblBacteria; ABM40784; ABM40784; Ajs_0534.
DR KEGG; ajs:Ajs_0534; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_0_0_4; -.
DR OMA; NSFIKWR; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000645; 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.
DR TIGRFAMs; TIGR00671; baf; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Potassium; Reference proteome; Transferase.
FT CHAIN 1..258
FT /note="Type III pantothenate kinase"
FT /id="PRO_1000054355"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 7..14
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 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
SQ SEQUENCE 258 AA; 27735 MW; 9777A843C88F5FF0 CRC64;
MTFLAIDVGN TRLKWALFDA AQPGAGLLAH GAEFLDHIER LAEGPWSHLP APRHMLGCVV
AGDAVKRRVA EQMELWDVPA RWVVPSAQEA GVINGYDHPT RLGADRWVAM IGARHRLLAQ
GPARPLIVVM VGTAVTVEAL DAEGRFLGGL ILPGHGIMLR ALESGTAGLH VPTGEVRLFP
SNTSDALTSG GTYAIAGAVE RMYQHLRQHC GQEPACMMTG GAGWKMAPSM TRPFELVENL
IFDGLLEIAA RRFAELPA
