COAX_BURTA
ID COAX_BURTA Reviewed; 259 AA.
AC Q2T1M2;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=BTH_I0369;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC37407.1; -; Genomic_DNA.
DR RefSeq; WP_009893234.1; NZ_CP008785.1.
DR PDB; 4O5F; X-ray; 1.55 A; A/B=1-259.
DR PDB; 4O8K; X-ray; 1.70 A; A/B=1-259.
DR PDBsum; 4O5F; -.
DR PDBsum; 4O8K; -.
DR AlphaFoldDB; Q2T1M2; -.
DR SMR; Q2T1M2; -.
DR PRIDE; Q2T1M2; -.
DR EnsemblBacteria; ABC37407; ABC37407; BTH_I0369.
DR GeneID; 66545895; -.
DR KEGG; bte:BTH_I0369; -.
DR HOGENOM; CLU_066627_0_0_4; -.
DR OMA; NSFIKWR; -.
DR OrthoDB; 2039419at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000001930; 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 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 Nucleotide-binding; Potassium; Transferase.
FT CHAIN 1..259
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000270869"
FT ACT_SITE 102
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 100..103
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 15..24
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:4O5F"
FT HELIX 58..69
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:4O5F"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4O5F"
FT HELIX 101..113
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 118..133
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:4O5F"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4O5F"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:4O5F"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:4O8K"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4O5F"
FT HELIX 190..217
FT /evidence="ECO:0007829|PDB:4O5F"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:4O5F"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:4O5F"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:4O5F"
SQ SEQUENCE 259 AA; 27005 MW; 8EAC15B63218AC98 CRC64;
MSGVCLLIDA GNSRIKWALA DTGRHFVTSG AFEHADDTPD WSTLPAPRGA WISNVAGDAA
AARIDALIDA HWPALPRTVV RACAAQCGVT NGYAEPARLG SDRWAGLIGA HAAFPGEHLL
IATFGTATTL EALRADGRFT GGLIAPGWAL MMRSLGMHTA QLPTVSIDAA TSLLDELAAN
DAHAPFAIDT PHALSAGCLQ AQAGLIERAW RDLEKAWKAP VRLVLSGGAA DAIVRALTVP
HTRHDTLVLT GLALIAHSA
