COAA_HAEDU
ID COAA_HAEDU Reviewed; 316 AA.
AC Q7VPK9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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}; OrderedLocusNames=HD_0056;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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: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}.
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DR EMBL; AE017143; AAP95071.1; -; Genomic_DNA.
DR RefSeq; WP_010944125.1; NC_002940.2.
DR AlphaFoldDB; Q7VPK9; -.
DR SMR; Q7VPK9; -.
DR STRING; 233412.HD_0056; -.
DR EnsemblBacteria; AAP95071; AAP95071; HD_0056.
DR KEGG; hdu:HD_0056; -.
DR eggNOG; COG1072; Bacteria.
DR HOGENOM; CLU_053818_1_1_6; -.
DR OMA; RKYTQVS; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000001022; 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; -; 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 PANTHER; PTHR10285:SF139; PTHR10285:SF139; 1.
DR Pfam; PF00485; PRK; 1.
DR PIRSF; PIRSF000545; Pantothenate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00554; panK_bact; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..316
FT /note="Pantothenate kinase"
FT /id="PRO_0000194430"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
SQ SEQUENCE 316 AA; 36314 MW; 3AF5F87B62B4B7E4 CRC64;
MGLQTTKKIT PFLTFDRQQW AKLRKSVPLK LTEQDLKPLL SFNEELSLEE VSTIYLPLAR
LINYYIEENI KRQTVLHRFL GVKSPKVPYI ISLAGSVSVG KSTSARILQA LLCQWPVERK
VDLITTDGFL YPLAILQAKN LLNRKGFPES YDIHRLIKFV SDLKSGERNI KAPIYSHLTY
DIIPDRYSVV DQPEIVILEG LNVLQSGMNY PSSPHNVFVS DFVDFSIYVD ADEALLKSWY
IHRFLKFRCS AFSDPNSYFH HYAKLSEEQA VKTATTIWDE INGLNLKQNI VPSRERADLI
LVKGEDHAIQ TVKLRK