(data stored in ACNUC1104 zone)

SWISSPROT: COAX_SACEN

ID   COAX_SACEN              Reviewed;         265 AA.
AC   A4F6T2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 77.
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=SACE_0408;
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338;
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
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; AM420293; CAL99756.1; -; Genomic_DNA.
DR   RefSeq; WP_009946422.1; NZ_PDBV01000001.1.
DR   SMR; A4F6T2; -.
DR   STRING; 405948.SACE_0408; -.
DR   EnsemblBacteria; CAL99756; CAL99756; SACE_0408.
DR   KEGG; sen:SACE_0408; -.
DR   eggNOG; ENOG4105CGM; Bacteria.
DR   eggNOG; COG1521; LUCA.
DR   HOGENOM; HOG000066025; -.
DR   KO; K03525; -.
DR   OMA; HEPWLTL; -.
DR   OrthoDB; 2039419at2; -.
DR   BioCyc; SERY405948:SACE_RS02005-MONOMER; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000006728; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; A4F6T2.
DR   SWISS-2DPAGE; A4F6T2.
KW   ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm;
KW   Kinase; Metal-binding; Nucleotide-binding; Potassium;
KW   Reference proteome; Transferase.
FT   CHAIN         1    265       Type III pantothenate kinase.
FT                                /FTId=PRO_1000054409.
FT   NP_BIND       6     13       ATP. {ECO:0000255|HAMAP-Rule:MF_01274}.
FT   REGION      112    115       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
FT   ACT_SITE    114    114       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
FT   METAL       134    134       Monovalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
FT   BINDING     137    137       ATP. {ECO:0000255|HAMAP-Rule:MF_01274}.
FT   BINDING     189    189       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01274}.
SQ   SEQUENCE   265 AA;  28262 MW;  CCBEE62E7F2C3AB6 CRC64;
     MLLAIDVGNT NIVLGLYADE PAEGADPVLV RDWRMRTEPR MTADELALTV RGLLGSYADR
     ITGISALSTV PSLLRELRVM LGRYWTDVPR VVVEPGVRTG VPLLVDNPKE VGADRVINTL
     AAHHLHATNC VVVDFGTSTN IDAISAKGEF LGGAFAPGIE ISLDALASRA AQLRKVELVR
     PRSVIGKNTV ECLQSGILYG FAGQVDGLVR RIVAELESTH GGPTTVIGTG GLAPLVVTES
     DTISHHVPDL TLLGLRLVYD RNFGS
//

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