COAA_MYCLE
ID COAA_MYCLE Reviewed; 312 AA.
AC Q9X795;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Pantothenate kinase;
DE EC=2.7.1.33;
DE AltName: Full=Pantothenic acid kinase;
GN Name=coaA; OrderedLocusNames=ML1954; ORFNames=MLCB1222.23;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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 -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC {ECO:0000305}.
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DR EMBL; AL049491; CAB39829.1; -; Genomic_DNA.
DR EMBL; AL583923; CAC30909.1; -; Genomic_DNA.
DR PIR; E87153; E87153.
DR RefSeq; NP_302319.1; NC_002677.1.
DR RefSeq; WP_010908640.1; NC_002677.1.
DR AlphaFoldDB; Q9X795; -.
DR SMR; Q9X795; -.
DR STRING; 272631.ML1954; -.
DR EnsemblBacteria; CAC30909; CAC30909; CAC30909.
DR KEGG; mle:ML1954; -.
DR PATRIC; fig|272631.5.peg.3703; -.
DR Leproma; ML1954; -.
DR eggNOG; COG1072; Bacteria.
DR HOGENOM; CLU_053818_1_1_11; -.
DR OMA; RKYTQVS; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000806; 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; Reference proteome; Transferase.
FT CHAIN 1..312
FT /note="Pantothenate kinase"
FT /id="PRO_0000194438"
FT BINDING 97..104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 312 AA; 35492 MW; FBAEF9DD3F397871 CRC64;
MPRLSEPSPY VEFDRKQWRA LRMSTPLALT EEELIGLRGL GEQIDLLEVE EVYLPLARLI
HLQVAARQRL FAATAEFLGE PQQNPGRPVP FIIGVAGSVA VGKSTTARVL QALLARWDHH
TRVDLVTTDG FLYPNAELGR RNLMHRKGFP ESYNRRALMR FVTSVKSGAD YACAPVYSHL
RYDTIPGAKH VVRHPDILIL EGLNVLQTGP TLMVSDLFDF SLYVDARIQD IEQWYVSRFL
AMRGTAFADP ESHFHHYSAL TDSKAIIAAR EIWRSINRPN LVENILPTRP RATLVLRKDA
DHSINRLRLR KL
