COAA_ECOUT
ID COAA_ECOUT Reviewed; 316 AA.
AC Q1R5X9;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=UTI89_C3802;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA Gordon J.I.;
RT "Identification of genes subject to positive selection in uropathogenic
RT strains of Escherichia coli: a comparative genomics approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; 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 -!- SEQUENCE CAUTION:
CC Sequence=ABE09235.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000243; ABE09235.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000023081.1; NC_007946.1.
DR AlphaFoldDB; Q1R5X9; -.
DR SMR; Q1R5X9; -.
DR EnsemblBacteria; ABE09235; ABE09235; UTI89_C3802.
DR GeneID; 66672114; -.
DR KEGG; eci:UTI89_C3802; -.
DR HOGENOM; CLU_053818_1_1_6; -.
DR OMA; RKYTQVS; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000001952; 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 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..316
FT /note="Pantothenate kinase"
FT /id="PRO_0000325552"
FT BINDING 95..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
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
