COAA_COXBU
ID COAA_COXBU Reviewed; 318 AA.
AC Q83EV9;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_00215};
DE EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_00215};
DE AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_00215};
GN Name=coaA {ECO:0000255|HAMAP-Rule:MF_00215}; OrderedLocusNames=CBU_0199;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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_00215};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_00215}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00215}.
CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00215}.
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DR EMBL; AE016828; AAO89759.1; -; Genomic_DNA.
DR RefSeq; NP_819245.1; NC_002971.3.
DR RefSeq; WP_010957432.1; NC_002971.4.
DR PDB; 3TQC; X-ray; 2.30 A; A/B=1-318.
DR PDBsum; 3TQC; -.
DR AlphaFoldDB; Q83EV9; -.
DR SMR; Q83EV9; -.
DR STRING; 227377.CBU_0199; -.
DR DNASU; 1208075; -.
DR EnsemblBacteria; AAO89759; AAO89759; CBU_0199.
DR GeneID; 1208075; -.
DR KEGG; cbu:CBU_0199; -.
DR PATRIC; fig|227377.7.peg.197; -.
DR eggNOG; COG1072; Bacteria.
DR HOGENOM; CLU_053818_1_1_6; -.
DR OMA; RKYTQVS; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004594; F:pantothenate kinase activity; IBA:GO_Central.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd02025; PanK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00215; Pantothen_kinase_1; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004566; PanK.
DR InterPro; IPR006083; PRK/URK.
DR PANTHER; PTHR10285:SF139; PTHR10285:SF139; 1.
DR Pfam; PF00485; PRK; 1.
DR PIRSF; PIRSF000545; Pantothenate_kin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00554; panK_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..318
FT /note="Pantothenate kinase"
FT /id="PRO_0000194425"
FT BINDING 96..103
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
FT STRAND 12..17
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 34..39
FT /evidence="ECO:0007829|PDB:3TQC"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 56..81
FT /evidence="ECO:0007829|PDB:3TQC"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:3TQC"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 134..139
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:3TQC"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:3TQC"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:3TQC"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:3TQC"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:3TQC"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:3TQC"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:3TQC"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 234..250
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:3TQC"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:3TQC"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:3TQC"
FT STRAND 310..316
FT /evidence="ECO:0007829|PDB:3TQC"
SQ SEQUENCE 318 AA; 36922 MW; C6836DD88B83785B CRC64;
MTVKPELNEI TPYLQFNRQQ WGNFRKDTPL TLTESDLDKL QGQIEIVSLK EVTEIYLPLS
RLLSFYVTAR QTLQQATYQF LGKPEPKVPY IIGIAGSVAV GKSTTSRVLK ALLSRWPDHP
NVEVITTDGF LYSNAKLEKQ GLMKRKGFPE SYDMPSLLRV LNAIKSGQRN VRIPVYSHHY
YDIVRGQYEI VDQPDIVILE GLNILQTGVR KTLQQLQVFV SDFFDFSLFV DAQAQVIQKW
YIDRVLSFWR TTFKDPHSYF HYLTQMSETE VAAFAKHVWN EINKVNLMEN ILPYKNRAQL
ILEKAADHSI QKVYLRKI
