COAW_STAHJ
ID COAW_STAHJ Reviewed; 266 AA.
AC Q4L811;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Type II pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_01273};
DE EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_01273};
DE AltName: Full=PanK-II {ECO:0000255|HAMAP-Rule:MF_01273};
DE AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_01273};
GN Name=coaW {ECO:0000255|HAMAP-Rule:MF_01273}; OrderedLocusNames=SH0905;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01273}.
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_01273};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_01273}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01273}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01273}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01273}.
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DR EMBL; AP006716; BAE04214.1; -; Genomic_DNA.
DR RefSeq; WP_011275216.1; NC_007168.1.
DR AlphaFoldDB; Q4L811; -.
DR SMR; Q4L811; -.
DR STRING; 279808.SH0905; -.
DR EnsemblBacteria; BAE04214; BAE04214; SH0905.
DR GeneID; 58062912; -.
DR KEGG; sha:SH0905; -.
DR eggNOG; COG5146; Bacteria.
DR HOGENOM; CLU_087521_1_0_9; -.
DR OMA; VKHIYKD; -.
DR OrthoDB; 1362749at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000543; 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_01273; Pantothen_kinase_2; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004567; Type_II_PanK.
DR InterPro; IPR011602; Type_II_PanK_bac.
DR PANTHER; PTHR12280; PTHR12280; 1.
DR Pfam; PF03630; Fumble; 1.
DR PIRSF; PIRSF036940; PanK_bac_aCoA; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..266
FT /note="Type II pantothenate kinase"
FT /id="PRO_0000261354"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 121..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
SQ SEQUENCE 266 AA; 28628 MW; FD5049A783A6AD9E CRC64;
MKVGIDAGGT LIKIVQESQQ GRSYETKLTT NISEVIAWLN ANTFESISLT GGNAGVIAEN
LNVDATIFVE FDASSKGLGM LLKEQGHHID EYIFANVGTG TSLHYFDGKQ QRRVGGVGTG
GGMIQGLGYL LSQITDYEAL TNLAQSGDRD TIDLKVKHIY KDTEPPIPGE LTAANFGNVL
HNLDVDFSPA NKLASVVGVV GEVITTMAIT VARENKTENV VYIGSSFNNN PLLREVIEDY
TVLRGFKPYY IENGAFSGAL GAIYLN
