ID   COAA_MYCTA              Reviewed;         312 AA.
AC   A5U1D9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_00215};
DE            EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_00215};
DE   AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_00215};
GN   Name=coaA {ECO:0000255|HAMAP-Rule:MF_00215}; OrderedLocusNames=MRA_1103;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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_00215};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_00215}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00215}.
CC   -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00215}.
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DR   EMBL; CP000611; ABQ72839.1; -; Genomic_DNA.
DR   RefSeq; WP_003405790.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U1D9; -.
DR   SMR; A5U1D9; -.
DR   STRING; 419947.MRA_1103; -.
DR   EnsemblBacteria; ABQ72839; ABQ72839; MRA_1103.
DR   GeneID; 45425066; -.
DR   KEGG; mra:MRA_1103; -.
DR   eggNOG; COG0572; Bacteria.
DR   HOGENOM; CLU_053818_1_1_11; -.
DR   OMA; RKYTQVS; -.
DR   OrthoDB; 1793376at2; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000001988; 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   CDD; cd02025; PanK; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00215; Pantothen_kinase_1; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004566; PanK.
DR   InterPro; IPR006083; PRK/URK.
DR   PANTHER; PTHR10285:SF139; PTHR10285:SF139; 1.
DR   Pfam; PF00485; PRK; 1.
DR   PIRSF; PIRSF000545; Pantothenate_kin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00554; panK_bact; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..312
FT                   /note="Pantothenate kinase"
FT                   /id="PRO_1000043232"
FT   BINDING         97..104
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   312 AA;  35657 MW;  F075B543AE75788D CRC64;
     MSRLSEPSPY VEFDRRQWRA LRMSTPLALT EEELVGLRGL GEQIDLLEVE EVYLPLARLI
     HLQVAARQRL FAATAEFLGE PQQNPDRPVP FIIGVAGSVA VGKSTTARVL QALLARWDHH
     PRVDLVTTDG FLYPNAELQR RNLMHRKGFP ESYNRRALMR FVTSVKSGSD YACAPVYSHL
     HYDIIPGAEQ VVRHPDILIL EGLNVLQTGP TLMVSDLFDF SLYVDARIED IEQWYVSRFL
     AMRTTAFADP ESHFHHYAAF SDSQAVVAAR EIWRTINRPN LVENILPTRP RATLVLRKDA
     DHSINRLRLR KL