COAX_THEMA
ID COAX_THEMA Reviewed; 246 AA.
AC Q9WZY5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
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; OrderedLocusNames=TM_0883;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, SUBUNIT, AND KINETIC
RP PARAMETERS.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
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).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000269|PubMed:16855243}.
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; Evidence={ECO:0000250};
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250};
CC Note=A monovalent cation. Ammonium or potassium. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for pantothenate (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:16855243};
CC KM=6.0 mM for ATP (at 50 degrees Celsius)
CC {ECO:0000269|PubMed:16855243};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16855243}.
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; AE000512; AAD35964.1; -; Genomic_DNA.
DR PIR; D72320; D72320.
DR RefSeq; NP_228691.1; NC_000853.1.
DR RefSeq; WP_004080709.1; NZ_CP011107.1.
DR PDB; 2GTD; X-ray; 2.00 A; A/B/C/D/E/F=1-245.
DR PDB; 3BEX; X-ray; 1.51 A; A/B/C/D/E/F=1-246.
DR PDB; 3BF1; X-ray; 2.30 A; A/B/C/D/E/F=1-246.
DR PDB; 3BF3; X-ray; 1.63 A; A/B/C/D/E/F=1-246.
DR PDBsum; 2GTD; -.
DR PDBsum; 3BEX; -.
DR PDBsum; 3BF1; -.
DR PDBsum; 3BF3; -.
DR AlphaFoldDB; Q9WZY5; -.
DR SMR; Q9WZY5; -.
DR STRING; 243274.THEMA_00220; -.
DR EnsemblBacteria; AAD35964; AAD35964; TM_0883.
DR KEGG; tma:TM0883; -.
DR eggNOG; COG1521; Bacteria.
DR InParanoid; Q9WZY5; -.
DR OMA; HEPWLTL; -.
DR OrthoDB; 2039419at2; -.
DR BRENDA; 2.7.1.33; 6331.
DR SABIO-RK; Q9WZY5; -.
DR UniPathway; UPA00241; UER00352.
DR EvolutionaryTrace; Q9WZY5; -.
DR Proteomes; UP000008183; 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..246
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000267598"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 103..106
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:3BEX"
FT STRAND 9..22
FT /evidence="ECO:0007829|PDB:3BEX"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3BEX"
FT HELIX 36..47
FT /evidence="ECO:0007829|PDB:3BEX"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:3BEX"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:3BEX"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:3BEX"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:3BEX"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:3BEX"
FT HELIX 104..116
FT /evidence="ECO:0007829|PDB:3BEX"
FT STRAND 121..136
FT /evidence="ECO:0007829|PDB:3BEX"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:3BEX"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:3BEX"
FT STRAND 173..178
FT /evidence="ECO:0007829|PDB:3BEX"
FT HELIX 179..206
FT /evidence="ECO:0007829|PDB:3BEX"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:3BEX"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:3BEX"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3BEX"
FT HELIX 234..244
FT /evidence="ECO:0007829|PDB:3BEX"
SQ SEQUENCE 246 AA; 27154 MW; 9E0309AD462CF266 CRC64;
MYLLVDVGNT HSVFSITEDG KTFRRWRLST GVFQTEDELF SHLHPLLGDA MREIKGIGVA
SVVPTQNTVI ERFSQKYFHI SPIWVKAKNG CVKWNVKNPS EVGADRVANV VAFVKEYGKN
GIIIDMGTAT TVDLVVNGSY EGGAILPGFF MMVHSLFRGT AKLPLVEVKP ADFVVGKDTE
ENIRLGVVNG SVYALEGIIG RIKEVYGDLP VVLTGGQSKI VKDMIKHEIF DEDLTIKGVY
HFCFGD
