COAA_KLEP3
ID COAA_KLEP3 Reviewed; 316 AA.
AC B5XYG3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=KPK_5321;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000964; ACI11207.1; -; Genomic_DNA.
DR PDB; 4F7W; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-316.
DR PDB; 4GI7; X-ray; 1.95 A; A/B/C/D/E/F/G/H=1-316.
DR PDB; 4NE2; X-ray; 1.90 A; A/B=1-316.
DR PDBsum; 4F7W; -.
DR PDBsum; 4GI7; -.
DR PDBsum; 4NE2; -.
DR AlphaFoldDB; B5XYG3; -.
DR SMR; B5XYG3; -.
DR EnsemblBacteria; ACI11207; ACI11207; KPK_5321.
DR KEGG; kpe:KPK_5321; -.
DR HOGENOM; CLU_053818_1_1_6; -.
DR OMA; RKYTQVS; -.
DR OrthoDB; 1793376at2; -.
DR BRENDA; 2.7.1.33; 2814.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000001734; Chromosome.
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 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; Transferase.
FT CHAIN 1..316
FT /note="Pantothenate kinase"
FT /id="PRO_1000099933"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 17..21
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:4GI7"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 55..80
FT /evidence="ECO:0007829|PDB:4NE2"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4NE2"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:4GI7"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:4NE2"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:4NE2"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:4NE2"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:4NE2"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4NE2"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:4NE2"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:4NE2"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 233..250
FT /evidence="ECO:0007829|PDB:4NE2"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:4NE2"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:4NE2"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:4NE2"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:4NE2"
SQ SEQUENCE 316 AA; 36214 MW; C5237900E1764043 CRC64;
MSQKEQTLMT PYLQFNRHQW AALRDSVPMT LTEDEITRLK GINEDLSLEE VAEIYLPLSR
LLNFYISSNL RRQAVLEQFL GTNGQRIPYI ISIAGSVAVG KSTTARVLQA LLSRWPEHRH
VELITTDGFL HPNSVLKERG LMKKKGFPQS YDMHRLVKFV SDLKSGVPQA TAPVYSHLIY
DVIPDGDKTV AQPDILILEG LNVLQSGMDY PHDPHHVFVS DFVDFSIYVD APEELLKSWY
INRFLKFREG AFTDPDSYFH NYAKLSKEEA VDIATSLWNE INLMNLKENI LPTRERASLI
MTKSANHSVN QVRLRK
