COAA_ECOLI
ID COAA_ECOLI Reviewed; 316 AA.
AC P0A6I3; P15044; Q2M8R5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Pantothenate kinase;
DE EC=2.7.1.33;
DE AltName: Full=Pantothenic acid kinase;
DE AltName: Full=Rts protein;
GN Name=coaA; Synonyms=panK, rts; OrderedLocusNames=b3974, JW3942;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1328157; DOI=10.1128/jb.174.20.6411-6417.1992;
RA Song W.-J., Jackowski S.;
RT "Cloning, sequencing, and expression of the pantothenate kinase (coaA) gene
RT of Escherichia coli.";
RL J. Bacteriol. 174:6411-6417(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1311303; DOI=10.1128/jb.174.5.1705-1706.1992;
RA Song W.-J., Jackowski S.;
RT "coaA and rts are allelic and located at kilobase 3532 on the Escherichia
RT coli physical map.";
RL J. Bacteriol. 174:1705-1706(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3073109; DOI=10.1016/0378-1119(88)90189-8;
RA Flamm J.A., Friesen J.D., Otsuka A.J.;
RT "The nucleotide sequence of the Escherichia coli rts gene.";
RL Gene 74:555-558(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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 -!- ACTIVITY REGULATION: Regulated by feedback inhibition by CoA and its
CC thioesters.
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23591.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA76838.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M36321; AAA76838.1; ALT_INIT; Genomic_DNA.
DR EMBL; M90071; AAA23590.1; -; Genomic_DNA.
DR EMBL; M90071; AAA23591.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00006; AAC43076.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76952.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77341.1; -; Genomic_DNA.
DR PIR; A45727; BVECRS.
DR RefSeq; NP_418405.1; NC_000913.3.
DR RefSeq; WP_000023081.1; NZ_STEB01000072.1.
DR PDB; 1ESM; X-ray; 2.50 A; A/B/C/D=1-316.
DR PDB; 1ESN; X-ray; 2.60 A; A/B/C/D=1-316.
DR PDB; 1SQ5; X-ray; 2.20 A; A/B/C/D=9-316.
DR PDBsum; 1ESM; -.
DR PDBsum; 1ESN; -.
DR PDBsum; 1SQ5; -.
DR AlphaFoldDB; P0A6I3; -.
DR SMR; P0A6I3; -.
DR IntAct; P0A6I3; 2.
DR STRING; 511145.b3974; -.
DR ChEMBL; CHEMBL5092; -.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB01783; Pantothenic acid.
DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DR jPOST; P0A6I3; -.
DR PaxDb; P0A6I3; -.
DR PRIDE; P0A6I3; -.
DR EnsemblBacteria; AAC76952; AAC76952; b3974.
DR EnsemblBacteria; BAE77341; BAE77341; BAE77341.
DR GeneID; 66672114; -.
DR GeneID; 948479; -.
DR KEGG; ecj:JW3942; -.
DR KEGG; eco:b3974; -.
DR PATRIC; fig|511145.12.peg.4091; -.
DR EchoBASE; EB0915; -.
DR eggNOG; COG1072; Bacteria.
DR HOGENOM; CLU_053818_1_1_6; -.
DR InParanoid; P0A6I3; -.
DR OMA; RKYTQVS; -.
DR PhylomeDB; P0A6I3; -.
DR BioCyc; EcoCyc:PANTOTHENATE-KIN-MON; -.
DR BioCyc; MetaCyc:PANTOTHENATE-KIN-MON; -.
DR BRENDA; 2.7.1.33; 2026.
DR SABIO-RK; P0A6I3; -.
DR UniPathway; UPA00241; UER00352.
DR EvolutionaryTrace; P0A6I3; -.
DR PRO; PR:P0A6I3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050165; F:pantetheine kinase activity; IDA:EcoCyc.
DR GO; GO:0004594; F:pantothenate kinase activity; IDA:EcoCyc.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IMP:EcoCyc.
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..316
FT /note="Pantothenate kinase"
FT /id="PRO_0000194426"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1SQ5"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:1ESN"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 55..80
FT /evidence="ECO:0007829|PDB:1SQ5"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:1SQ5"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1ESM"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:1SQ5"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1SQ5"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1SQ5"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:1SQ5"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1SQ5"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1SQ5"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:1SQ5"
FT STRAND 224..230
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:1SQ5"
FT TURN 250..253
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 267..280
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 291..296
FT /evidence="ECO:0007829|PDB:1SQ5"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:1SQ5"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1SQ5"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:1SQ5"
SQ SEQUENCE 316 AA; 36360 MW; DDDC1922C5C52A70 CRC64;
MSIKEQTLMT PYLQFDRNQW AALRDSVPMT LSEDEIARLK GINEDLSLEE VAEIYLPLSR
LLNFYISSNL RRQAVLEQFL GTNGQRIPYI ISIAGSVAVG KSTTARVLQA LLSRWPEHRR
VELITTDGFL HPNQVLKERG LMKKKGFPES YDMHRLVKFV SDLKSGVPNV TAPVYSHLIY
DVIPDGDKTV VQPDILILEG LNVLQSGMDY PHDPHHVFVS DFVDFSIYVD APEDLLQTWY
INRFLKFREG AFTDPDSYFH NYAKLTKEEA IKTAMTLWKE INWLNLKQNI LPTRERASLI
LTKSANHAVE EVRLRK
