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Database: UniProt
Entry: A0A3B7D4M9_9ACTN
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ID   A0A3B7D4M9_9ACTN        Unreviewed;       313 AA.
AC   A0A3B7D4M9;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=C6I20_01700 {ECO:0000313|EMBL:AXT84033.1};
OS   Aeromicrobium sp. A1-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=2107713 {ECO:0000313|EMBL:AXT84033.1, ECO:0000313|Proteomes:UP000257855};
RN   [1] {ECO:0000313|EMBL:AXT84033.1, ECO:0000313|Proteomes:UP000257855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1-2 {ECO:0000313|EMBL:AXT84033.1,
RC   ECO:0000313|Proteomes:UP000257855};
RA   Liao L., Chen B.;
RT   "Complete genome of Aeromicrobium sp. A1-2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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; CP027482; AXT84033.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B7D4M9; -.
DR   KEGG; aeb:C6I20_01700; -.
DR   OrthoDB; 1550976at2; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000257855; 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:AXT84033.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257855};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00215}.
FT   DOMAIN          87..229
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   BINDING         92..99
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   313 AA;  35298 MW;  C2A76DCBE8DE8445 CRC64;
     MARDQSPYVE LERAAWAELA GDAPQPLQPA EIERVRGLGD ELDLEEVRQV YLPMTQLISM
     RVRLAGALYQ ATEAFLHEPQ TRRTPFVIGI AGSVAVGKST TARLLKELLS HSPQHPVVEL
     VTTDGFLFPN DELERRGLLD RKGFPESYDR KALLRFVMEV KSGVEVVTAP IYSHLTYDRT
     DEVVTLKKPD IVIVEGLNVL APARPRGDGS PGLAVSDFFD FSIYVDASGK DLRRWYIDRF
     LSLRKTAFAD PESYFHRYSA LTDDEAVARA GHLWDTINWP NLRENIATTR GRASLVLRKG
     ADHSVDWVRL RKL
//
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