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Database: UniProt
Entry: A0A060JGY8_9MICO
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ID   A0A060JGY8_9MICO        Unreviewed;       309 AA.
AC   A0A060JGY8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
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   ORFNames=Rhola_00012070 {ECO:0000313|EMBL:AIC48000.1};
OS   Rhodoluna lacicola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Luna cluster; Luna-1 subcluster; Rhodoluna.
OX   NCBI_TaxID=529884 {ECO:0000313|EMBL:AIC48000.1, ECO:0000313|Proteomes:UP000067708};
RN   [1] {ECO:0000313|EMBL:AIC48000.1, ECO:0000313|Proteomes:UP000067708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-Ta8 {ECO:0000313|EMBL:AIC48000.1,
RC   ECO:0000313|Proteomes:UP000067708};
RX   PubMed=24984700; DOI=10.1099/ijs.0.065292-0;
RA   Hahn M., Schmidt J., Taipale S.J., Doolittle W.F., Koll U.;
RT   "Rhodoluna lacicola gen. nov., sp. nov., a planktonic freshwater bacterium
RT   with stream-lined genome.";
RL   Int. J. Syst. Evol. Microbiol. 64:3254-3263(2014).
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|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00215, 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; CP007490; AIC48000.1; -; Genomic_DNA.
DR   RefSeq; WP_038503139.1; NZ_CP007490.1.
DR   AlphaFoldDB; A0A060JGY8; -.
DR   STRING; 529884.Rhola_00012070; -.
DR   KEGG; rla:Rhola_00012070; -.
DR   PATRIC; fig|529884.3.peg.1167; -.
DR   eggNOG; COG1072; Bacteria.
DR   HOGENOM; CLU_053818_1_1_11; -.
DR   OrthoDB; 1550976at2; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000067708; 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; 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   PANTHER; PTHR10285:SF139; PANTOTHENATE KINASE; 1.
DR   PANTHER; PTHR10285; URIDINE KINASE; 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:AIC48000.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067708};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000313|EMBL:AIC48000.1}.
FT   DOMAIN          86..226
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   BINDING         91..98
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   309 AA;  34920 MW;  5B21128D176170B0 CRC64;
     MSDALSPFNE ISREDWAVLG NSTELPLTES EIQQIRGLGD FLDIKEVQDV YLPLSRLLNL
     YVTEHQKLHR STSDFLGERA GRVPFIIGVA GSVAVGKSTV SRLLKELLSR WDGTPSVEMI
     TTDGFLHPNE ELERRGLMSR KGFPESYDRM ALLEFIADVK SGAKEVSAPV YSHLIYDIVA
     GQRQTIKNPD VLIVEGLNVL QSPGPGQYVA LSDFFDFKIY VDADTKNLTQ WFLDRFEKLR
     DTAFTNPASY FHRYAEMPHE KALARANEIW STINLPNLIE NILPTRSRAT LVLQKGAMHA
     VERVLLRKL
//
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