COAX_HELPY
ID COAX_HELPY Reviewed; 223 AA.
AC O25533;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Type III pantothenate kinase;
DE EC=2.7.1.33;
DE AltName: Full=PanK-III;
DE AltName: Full=Pantothenic acid kinase;
GN Name=coaX; Synonyms=coaA; OrderedLocusNames=HP_0862;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP FUNCTION, CHARACTERIZATION, ACTIVITY REGULATION, AND KINETIC PARAMETERS.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=15795230; DOI=10.1074/jbc.c500044200;
RA Brand L.A., Strauss E.;
RT "Characterization of a new pantothenate kinase isoform from Helicobacter
RT pylori.";
RL J. Biol. Chem. 280:20185-20188(2005).
RN [3]
RP MUTAGENESIS OF ASP-17; ASP-87 AND ASP-102.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=16855243; DOI=10.1128/jb.00469-06;
RA Yang K., Eyobo Y., Brand L.A., Martynowski D., Tomchick D., Strauss E.,
RA Zhang H.;
RT "Crystal structure of a type III pantothenate kinase: insight into the
RT mechanism of an essential coenzyme A biosynthetic enzyme universally
RT distributed in bacteria.";
RL J. Bacteriol. 188:5532-5540(2006).
RN [4]
RP FUNCTION, AND COFACTOR.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=16905099; DOI=10.1016/j.str.2006.06.008;
RA Hong B.S., Yun M.K., Zhang Y.-M., Chohnan S., Rock C.O., White S.W.,
RA Jackowski S., Park H.-W., Leonardi R.;
RT "Prokaryotic type II and type III pantothenate kinases: the same monomer
RT fold creates dimers with distinct catalytic properties.";
RL Structure 14:1251-1261(2006).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. Can also utilize CTP or GTP instead of
CC ATP as a phosphoryl donor, albeit to a lesser extent.
CC {ECO:0000269|PubMed:15795230, ECO:0000269|PubMed:16905099}.
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;
CC -!- COFACTOR:
CC Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC Evidence={ECO:0000269|PubMed:16905099};
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:16905099};
CC Note=Monovalent cations. Ammonium or potassium.
CC {ECO:0000269|PubMed:16905099};
CC -!- ACTIVITY REGULATION: Not regulated by feedback inhibition by CoA and
CC its thioesters as described for many other pantothenate kinases. Not
CC inhibited by N-pentylpantothenamide (N5-Pan), and this compound cannot
CC act as a substrate either. {ECO:0000269|PubMed:15795230}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=101 uM for pantothenate {ECO:0000269|PubMed:15795230};
CC KM=9.6 mM for ATP {ECO:0000269|PubMed:15795230};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC O25533; O26009: tmk; NbExp=2; IntAct=EBI-528040, EBI-528054;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC {ECO:0000305}.
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DR EMBL; AE000511; AAD07916.1; -; Genomic_DNA.
DR PIR; F64627; F64627.
DR RefSeq; NP_207656.1; NC_000915.1.
DR RefSeq; WP_001111589.1; NC_018939.1.
DR AlphaFoldDB; O25533; -.
DR SMR; O25533; -.
DR DIP; DIP-3271N; -.
DR IntAct; O25533; 13.
DR MINT; O25533; -.
DR STRING; 85962.C694_04415; -.
DR PaxDb; O25533; -.
DR DNASU; 899391; -.
DR EnsemblBacteria; AAD07916; AAD07916; HP_0862.
DR KEGG; hpy:HP_0862; -.
DR PATRIC; fig|85962.47.peg.916; -.
DR eggNOG; COG1521; Bacteria.
DR OMA; FHLETDY; -.
DR PhylomeDB; O25533; -.
DR BioCyc; MetaCyc:HP0862-MON; -.
DR SABIO-RK; O25533; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000429; 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 1: Evidence at protein level;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome; Transferase.
FT CHAIN 1..223
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000267545"
FT ACT_SITE 87
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85..88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MUTAGEN 17
FT /note="D->N: 5% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16855243"
FT MUTAGEN 87
FT /note="D->E: 3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16855243"
FT MUTAGEN 87
FT /note="D->N: 3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16855243"
FT MUTAGEN 102
FT /note="D->N,E: 3% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:16855243"
SQ SEQUENCE 223 AA; 24655 MW; C1D13E8BEC1EB9AF CRC64;
MPARQSFTDL KNLVLCDIGN TRIHFAQNYQ LFSSAKEDLK RLGIQKEIFY ISVNEENEKA
LLNCYPNAKN IAGFFHLETD YVGLGIDRQM ACLAVNNGVV VDAGSAITID LIKEGKHLGG
CILPGLAQYI HAYKKSAKIL EQPFKALDSL EVLPKSTRDA VNYGMVLSVI ACIQHLAKNQ
KIYLCGGDAK YLSAFLPHSV CKERLVFDGM EIALKKAGIL ECK
