SWISSPROT: COAX_LISMF

ID   COAX_LISMF              Reviewed;         259 AA.
AC   Q724J2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 87.
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};
GN   OrderedLocusNames=LMOf2365_0232;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(2004).
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,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; EC=2.7.1.33; Evidence={ECO:0000255|HAMAP-
CC         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.
CC       {ECO:0000255|HAMAP-Rule:MF_01274};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-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}.
DR   EMBL; AE017262; AAT03019.1; -; Genomic_DNA.
DR   RefSeq; WP_003725746.1; NC_002973.6.
DR   SMR; Q724J2; -.
DR   EnsemblBacteria; AAT03019; AAT03019; LMOf2365_0232.
DR   KEGG; lmf:LMOf2365_0232; -.
DR   HOGENOM; HOG000066025; -.
DR   KO; K03525; -.
DR   OMA; HEPWLTL; -.
DR   BioCyc; LMON265669:G1G0V-231-MONOMER; -.
DR   UniPathway; UPA00241; UER00352.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR   InterPro; IPR004619; Type_III_PanK.
DR   PANTHER; PTHR34265; PTHR34265; 1.
DR   Pfam; PF03309; Pan_kinase; 1.
DR   TIGRFAMs; TIGR00671; baf; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q724J2.
DR   SWISS-2DPAGE; Q724J2.
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Metal-binding; Nucleotide-binding; Potassium; Transferase.
FT   CHAIN         1    259       Type III pantothenate kinase.
FT                                /FTId=PRO_0000267558.
FT   NP_BIND       6     13       ATP. {ECO:0000255|HAMAP-Rule:MF_01274}.
FT   REGION      107    110       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
FT   ACT_SITE    109    109       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
FT   METAL       129    129       Monovalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
FT   BINDING     132    132       ATP. {ECO:0000255|HAMAP-Rule:MF_01274}.
FT   BINDING     184    184       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
SQ   SEQUENCE   259 AA;  28181 MW;  6810695C23F25DEC CRC64;
     MILVIDVGNT NCTVGVYEKQ KLLKHWRMTT DRHRTSDELG MTVLNFFSYA NLTPSDIQGI
     IISSVVPPIM HAMETMCVRY FNIRPLIVGP GIKTGLNLKV DNPREIGSDR IVNAVAASEE
     YGTPVIVVDF GTATTFCYID ESGVYQGGAI APGIMISTEA LYNRAAKLPR VDIAESNQII
     GKSTVASMQA GIFYGFVGQC EGIIAEIKKQ SNASPVVVAT GGLARMITEK SSAVDILDPF
     LTLKGLELLY RRNKPTTEK
//