(data stored in ACNUC7421 zone)

SWISSPROT: COAX_PARXL

ID   COAX_PARXL              Reviewed;         270 AA.
AC   Q146G6;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Type III pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_01274};
DE            EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_01274};
DE   AltName: Full=PanK-III {ECO:0000255|HAMAP-Rule:MF_01274};
DE   AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_01274};
GN   Name=coaX {ECO:0000255|HAMAP-Rule:MF_01274};
GN   OrderedLocusNames=Bxeno_A0235; ORFNames=Bxe_A4227;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC       first step in CoA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP
CC         + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; EC=2.7.1.33; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01274};
CC   -!- COFACTOR:
CC       Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01274};
CC       Note=A monovalent cation. Ammonium or potassium.
CC       {ECO:0000255|HAMAP-Rule:MF_01274};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01274}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01274}.
CC   -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01274}.
DR   EMBL; CP000270; ABE28773.1; -; Genomic_DNA.
DR   RefSeq; WP_011486614.1; NZ_CP008760.1.
DR   SMR; Q146G6; -.
DR   STRING; 266265.Bxe_A4227; -.
DR   EnsemblBacteria; ABE28773; ABE28773; Bxe_A4227.
DR   GeneID; 4004271; -.
DR   KEGG; bxb:DR64_1904; -.
DR   KEGG; bxe:Bxe_A4227; -.
DR   PATRIC; fig|266265.5.peg.248; -.
DR   eggNOG; ENOG4108194; Bacteria.
DR   eggNOG; COG1521; LUCA.
DR   HOGENOM; HOG000066026; -.
DR   KO; K03525; -.
DR   OMA; NSFIKWR; -.
DR   OrthoDB; 2039419at2; -.
DR   BioCyc; BXEN266265:BXE_RS01170-MONOMER; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000001817; Chromosome 1.
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   HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR   InterPro; IPR004619; Type_III_PanK.
DR   PANTHER; PTHR34265; PTHR34265; 1.
DR   Pfam; PF03309; Pan_kinase; 1.
DR   TIGRFAMs; TIGR00671; baf; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q146G6.
DR   SWISS-2DPAGE; Q146G6.
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Kinase; Nucleotide-binding; Potassium; Reference proteome;
KW   Transferase.
FT   CHAIN         1    270       Type III pantothenate kinase.
FT                                /FTId=PRO_0000270870.
FT   NP_BIND      11     18       ATP. {ECO:0000255|HAMAP-Rule:MF_01274}.
FT   REGION      103    106       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
FT   ACT_SITE    105    105       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
FT   BINDING      96     96       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
FT   BINDING     129    129       ATP. {ECO:0000255|HAMAP-Rule:MF_01274}.
FT   BINDING     195    195       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
SQ   SEQUENCE   270 AA;  28053 MW;  30313EBDCB01FF86 CRC64;
     MTSGAPCLLI DAGNSRIKWA LVQAGGSQIA SGALTHGGEH QPDWLSLPTP GGAWLSNVAG
     ESVARRIAAL LEARWPQLPL TTISACAQQC GVTNSYTAPH MLGSDRWAGL IGAHAAFPGE
     HLLIATFGTA TTLEALRADG CFVGGLIAPG WTLMMRSLGE HTAQLPTLDA SAARGLLDGS
     TRDAARRGPF FATDTPRSLS AGCTLAQAGL VERMWRDLQD EWQVPVRLVV SGGAVDEVAS
     ALKVPHTRHD SLVLSGLALI AAGRAAERGA
//

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