COAX_HELPH
ID COAX_HELPH Reviewed; 223 AA.
AC Q1CT10;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Type III pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_01274};
DE EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_01274};
DE AltName: Full=PanK-III {ECO:0000255|HAMAP-Rule:MF_01274};
DE AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_01274};
GN Name=coaX {ECO:0000255|HAMAP-Rule:MF_01274}; OrderedLocusNames=HPAG1_0845;
OS Helicobacter pylori (strain HPAG1).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=357544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPAG1;
RX PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA Gordon J.I.;
RT "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT pylori strain: evolution during disease progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01274}.
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_01274};
CC -!- COFACTOR:
CC Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC Note=A monovalent cation. Ammonium or potassium. {ECO:0000255|HAMAP-
CC Rule:MF_01274};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01274}.
CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01274}.
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DR EMBL; CP000241; ABF84912.1; -; Genomic_DNA.
DR RefSeq; WP_001111566.1; NC_008086.1.
DR AlphaFoldDB; Q1CT10; -.
DR SMR; Q1CT10; -.
DR EnsemblBacteria; ABF84912; ABF84912; HPAG1_0845.
DR KEGG; hpa:HPAG1_0845; -.
DR HOGENOM; CLU_1213471_0_0_7; -.
DR OMA; FHLETDY; -.
DR OrthoDB; 2039419at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000008835; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004619; Type_III_PanK.
DR PANTHER; PTHR34265; PTHR34265; 1.
DR Pfam; PF03309; Pan_kinase; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00671; baf; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase; Metal-binding;
KW Nucleotide-binding; Potassium; Transferase.
FT CHAIN 1..223
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000267546"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 102
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
SQ SEQUENCE 223 AA; 24737 MW; CA1707744CA553D1 CRC64;
MPARQSFTDL KNLVLCDIGN THIHFAQNYQ LFSSAKEDLK RLGIQKEIFY ISVNEENEKA
LLNCYPNAKN IAGFFHLETD YIGLGIDRQM ACLAVNNGVV VDAGSAITID LVKEGKHLGG
CILPGLAQYI HAYKKSAKIL EQPFKTLDSL EILPKNTRDA VNYGMILSVI SCIQHLAKNQ
KIYLCGGDAK YLSAFLPHSV CKERLVFDGM EIALKKAGIL ECK
