ID COAA_BRUA2 Reviewed; 322 AA. AC Q2YQY6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_00215}; DE EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_00215}; DE AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_00215}; GN Name=coaA {ECO:0000255|HAMAP-Rule:MF_00215}; GN OrderedLocusNames=BAB1_2088; OS Brucella abortus (strain 2308). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=359391; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2308; RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005; RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.; RT "Whole-genome analyses of speciation events in pathogenic Brucellae."; RL Infect. Immun. 73:8353-8361(2005). 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_00215}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)- CC pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_00215}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00215}. CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00215}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AM040264; CAJ12044.1; -; Genomic_DNA. DR RefSeq; WP_002965153.1; NZ_KN046823.1. DR AlphaFoldDB; Q2YQY6; -. DR SMR; Q2YQY6; -. DR STRING; 359391.BAB1_2088; -. DR GeneID; 3788656; -. DR KEGG; bmf:BAB1_2088; -. DR PATRIC; fig|359391.11.peg.1322; -. DR HOGENOM; CLU_053818_1_1_5; -. DR PhylomeDB; Q2YQY6; -. DR UniPathway; UPA00241; UER00352. DR Proteomes; UP000002719; Chromosome I. 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; Coenzyme A biosynthesis; Cytoplasm; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..322 FT /note="Pantothenate kinase" FT /id="PRO_1000043213" FT BINDING 100..107 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00215" SQ SEQUENCE 322 AA; 37495 MW; D3EFE627DD4C7D0B CRC64; MWEKVDQLTP SRYSPYRFFS AQEWAAFRAD TPLTLTYEEV KRLRSLGDPI DLDEVRRIYL SLSRLLYAHV EASQLLFRQR QQFLNMEESY KTPFIIGVAG SVAVGKSTMA RILKELLARW PSSPKVDLVT TDGFLYPNAV LREQNMMERK GFPESYDIGA VLRFLSAIKA GMSRVRAPLY SHLSYDVLPG EYQIVDKPDI LIFEGINVLQ VRDLPEDGKM VPFVSDFFDF SIYIDADPRL IHKWYIDRFM RLRETAFRDP QSFFHRYSQL SQEAARSIAE GLWQNINMKN LNENILPTRP RADLILRKGS DHLIEEVALR KI //