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Database: UniProt
Entry: Q09B02_STIAD
LinkDB: Q09B02_STIAD
Original site: Q09B02_STIAD 
ID   Q09B02_STIAD            Unreviewed;       316 AA.
AC   Q09B02;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Pantothenate kinase {ECO:0000256|ARBA:ARBA00015080, ECO:0000256|HAMAP-Rule:MF_00215};
DE            EC=2.7.1.33 {ECO:0000256|ARBA:ARBA00012102, ECO:0000256|HAMAP-Rule:MF_00215};
DE   AltName: Full=Pantothenic acid kinase {ECO:0000256|HAMAP-Rule:MF_00215};
GN   Name=coaA {ECO:0000256|HAMAP-Rule:MF_00215,
GN   ECO:0000313|EMBL:EAU68903.1};
GN   OrderedLocusNames=STAUR_4597 {ECO:0000313|EMBL:ADO72377.1};
GN   ORFNames=STIAU_6846 {ECO:0000313|EMBL:EAU68903.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU68903.1, ECO:0000313|Proteomes:UP000032702};
RN   [1] {ECO:0000313|EMBL:EAU68903.1, ECO:0000313|Proteomes:UP000032702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU68903.1,
RC   ECO:0000313|Proteomes:UP000032702};
RA   Nierman W.C.;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADO72377.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO72377.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A., Kube M.,
RA   Reinhardt R., Klages S., Muller R., Ronning C.M., Nierman W.C.,
RA   Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
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:0000256|ARBA:ARBA00001206,
CC         ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5. {ECO:0000256|ARBA:ARBA00005225,
CC       ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00215,
CC       ECO:0000256|RuleBase:RU003530}.
CC   -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC       {ECO:0000256|ARBA:ARBA00006087, ECO:0000256|HAMAP-Rule:MF_00215,
CC       ECO:0000256|RuleBase:RU003530}.
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DR   EMBL; CP002271; ADO72377.1; -; Genomic_DNA.
DR   EMBL; AAMD01000011; EAU68903.1; -; Genomic_DNA.
DR   RefSeq; WP_002611455.1; NZ_AAMD01000011.1.
DR   STRING; 378806.STAUR_4597; -.
DR   KEGG; sur:STAUR_4597; -.
DR   PATRIC; fig|378806.16.peg.8226; -.
DR   eggNOG; COG1072; Bacteria.
DR   HOGENOM; CLU_053818_1_1_7; -.
DR   OrthoDB; 1550976at2; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000001351; Chromosome.
DR   Proteomes; UP000032702; Unassembled WGS sequence.
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; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00554; panK_bact; 1.
DR   Pfam; PF00485; PRK; 1.
DR   PIRSF; PIRSF000545; Pantothenate_kin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00215,
KW   ECO:0000256|RuleBase:RU003530};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000313|EMBL:EAU68903.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000313|EMBL:EAU68903.1}.
FT   DOMAIN          89..232
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   BINDING         94..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   316 AA;  36015 MW;  24337C15D034E008 CRC64;
     MFSSSSSPSL YVDFGREEWR ALRAATPLPL SEEEIERLRG LGEQLDLNEV VDVYLPLSRL
     LNLYVAATQN LWTAQQSFLG GFAQKVPFVI GIAGSVAVGK STTARILQAL LGRWPDHPRV
     ELVTTDGFLF PNNVLTKRGL MKRKGFPESY DRRALVRFLA DLKSGRSEVT TSIYSHHTYD
     IVQGEVKTIR QPDILILEGL NVLQTGPTDA ESVPRIFLSD FFDFSIYVDA NEQDIRRWYV
     NRFLRLWDTA FHDEKSFFRS FTKLTREEAI ARAETLWAEI NGPNLAQNIA PTRSRARLIL
     AKGPDHKVSR IRMRKL
//
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