COAX_BACAN
ID COAX_BACAN Reviewed; 262 AA.
AC Q81VX4; Q6I4X8; Q6KYM2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
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};
GN OrderedLocusNames=BA_0065, GBAA_0065, BAS0065;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=17323930; DOI=10.1021/bi062299p;
RA Nicely N.I., Parsonage D., Paige C., Newton G.L., Fahey R.C., Leonardi R.,
RA Jackowski S., Mallett T.C., Claiborne A.;
RT "Structure of the type III pantothenate kinase from Bacillus anthracis at
RT 2.0 A resolution: implications for coenzyme A-dependent redox biology.";
RL Biochemistry 46:3234-3245(2007).
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 ECO:0000269|PubMed:17323930}.
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; AE016879; AAP24120.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52403.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29143.2; -; Genomic_DNA.
DR RefSeq; NP_842634.1; NC_003997.3.
DR RefSeq; WP_000578367.1; NZ_WXXJ01000031.1.
DR RefSeq; YP_026352.1; NC_005945.1.
DR PDB; 2H3G; X-ray; 2.00 A; X=1-262.
DR PDBsum; 2H3G; -.
DR AlphaFoldDB; Q81VX4; -.
DR SMR; Q81VX4; -.
DR IntAct; Q81VX4; 1.
DR STRING; 261594.GBAA_0065; -.
DR BindingDB; Q81VX4; -.
DR ChEMBL; CHEMBL4295616; -.
DR DNASU; 1086632; -.
DR EnsemblBacteria; AAP24120; AAP24120; BA_0065.
DR EnsemblBacteria; AAT29143; AAT29143; GBAA_0065.
DR GeneID; 51131685; -.
DR GeneID; 59159628; -.
DR GeneID; 64204208; -.
DR KEGG; ban:BA_0065; -.
DR KEGG; bar:GBAA_0065; -.
DR KEGG; bat:BAS0065; -.
DR PATRIC; fig|198094.11.peg.62; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_1_0_9; -.
DR OMA; HEPWLTL; -.
DR BRENDA; 2.7.1.33; 634.
DR UniPathway; UPA00241; UER00352.
DR EvolutionaryTrace; Q81VX4; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Metal-binding; Nucleotide-binding; Potassium; Reference proteome;
KW Transferase.
FT CHAIN 1..262
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000267491"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 107..110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 129
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2H3G"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:2H3G"
FT STRAND 21..29
FT /evidence="ECO:0007829|PDB:2H3G"
FT HELIX 36..49
FT /evidence="ECO:0007829|PDB:2H3G"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:2H3G"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2H3G"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:2H3G"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:2H3G"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:2H3G"
FT STRAND 123..139
FT /evidence="ECO:0007829|PDB:2H3G"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:2H3G"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:2H3G"
FT HELIX 184..210
FT /evidence="ECO:0007829|PDB:2H3G"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2H3G"
FT HELIX 224..230
FT /evidence="ECO:0007829|PDB:2H3G"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2H3G"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:2H3G"
SQ SEQUENCE 262 AA; 29094 MW; 6ECC763CBCB9B4CC CRC64;
MIFVLDVGNT NAVLGVFEEG ELRQHWRMET DRHKTEDEYG MLVKQLLEHE GLSFEDVKGI
IVSSVVPPIM FALERMCEKY FKIKPLVVGP GIKTGLNIKY ENPREVGADR IVNAVAGIHL
YGSPLIIVDF GTATTYCYIN EEKHYMGGVI TPGIMISAEA LYSRAAKLPR IEITKPSSVV
GKNTVSAMQS GILYGYVGQV EGIVKRMKEE AKQEPKVIAT GGLAKLISEE SNVIDVVDPF
LTLKGLYMLY ERNANLQHEK GE
