COAA_STRZJ
ID COAA_STRZJ Reviewed; 306 AA.
AC C1CDI6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=SPJ_0776;
OS Streptococcus pneumoniae (strain JJA).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JJA;
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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; CP000919; ACO18702.1; -; Genomic_DNA.
DR RefSeq; WP_000180492.1; NC_012466.1.
DR AlphaFoldDB; C1CDI6; -.
DR SMR; C1CDI6; -.
DR EnsemblBacteria; ACO18702; ACO18702; SPJ_0776.
DR KEGG; sjj:SPJ_0776; -.
DR HOGENOM; CLU_053818_1_1_9; -.
DR OMA; RKYTQVS; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000002206; 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..306
FT /note="Pantothenate kinase"
FT /id="PRO_1000124811"
FT BINDING 91..98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
SQ SEQUENCE 306 AA; 35555 MW; 307002C489933CCE CRC64;
MTNEFLHFEK ISRQTWQSLH RKTTPPLTEE ELESIKSFND QISLQDVTDI YLPLAHLIQI
YKRTKEDLAF SKGIFLQRES KSQPFIIGVS GSVAVGKSTT SRLLQILLSR TFTDATVELV
TTDGFLYPNQ TLIEQGILNR KGFPESYDME ALLNFLDRIK NGQDVDIPVY SHEVYDIVPE
KKQSVKAADF VIVEGINVFQ NPQNDRLYIT DFFDFSIYVD AGVDDIESWY LDRFLKMLSL
AQNDPDSYYY RFTQMPIGEV ESFAHQVWIS INLTNLQNYI EPTRNRAEVI LHKSKNHEID
EIYLKK