(data stored in ACNUC7421 zone)

SWISSPROT: COAA_RHOPS

ID   COAA_RHOPS              Reviewed;         318 AA.
AC   Q13E42;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 80.
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=RPD_0409;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000283; ABE37647.1; -; Genomic_DNA.
DR   RefSeq; WP_011500835.1; NC_007958.1.
DR   SMR; Q13E42; -.
DR   STRING; 316057.RPD_0409; -.
DR   EnsemblBacteria; ABE37647; ABE37647; RPD_0409.
DR   KEGG; rpd:RPD_0409; -.
DR   eggNOG; ENOG4105CS9; Bacteria.
DR   eggNOG; COG1072; LUCA.
DR   HOGENOM; HOG000248571; -.
DR   KO; K00867; -.
DR   OMA; LMQRKGF; -.
DR   OrthoDB; 1793376at2; -.
DR   BioCyc; RPAL316057:RPD_RS02105-MONOMER; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000001818; 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   CDD; cd02025; PanK; 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;
DR   PRODOM; Q13E42.
DR   SWISS-2DPAGE; Q13E42.
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..318
FT                   /note="Pantothenate kinase"
FT                   /id="PRO_1000043245"
FT   NP_BIND         96..103
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   318 AA;  36267 MW;  4807D63CD37C17EC CRC64;
     MDARSELHHY NPYRVFSRSE WANLRQDTPM TLDLAEVSTL RSLHDRLDIT EVEEIYLPMS
     RLLSIHVGAM QQLYYAQRRF LGVVERKMPY IIGVAGSVAV GKSTTARVLQ ALLARWSPRP
     KVDLITTDGF LHPNALLERA GLMQKKGFPE SYDLPALLAF LSDIKSGRRK VRAPIYSHLT
     YDIVPNKFAV VDRPDILIVE GVNVLQTGRL PRDGKAVPVV SDFFDFSVYI DADEPVLRDW
     YIRRFLALRD TAFHDPRSYF HRYAPLSDEE ATATAIAIWE RTNLANLEDN ILPTRPRATL
     ILKKGADHVV DSVALRRL
//

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