(data stored in ACNUC30630 zone)

SWISSPROT: COAX_BIFAA

ID   COAX_BIFAA              Reviewed;         256 AA.
AC   A1A0M5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   11-DEC-2019, entry version 84.
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}; OrderedLocusNames=BAD_0477;
OS   Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS   E194a).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Bifidobacterium.
OX   NCBI_TaxID=367928;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA   Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA   Tanaka K., Watanabe K.;
RT   "Bifidobacterium adolescentis complete genome sequence.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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, 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_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. {ECO:0000255|HAMAP-
CC       Rule:MF_01274};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       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; AP009256; BAF39258.1; -; Genomic_DNA.
DR   RefSeq; WP_011742930.1; NC_008618.1.
DR   SMR; A1A0M5; -.
DR   EnsemblBacteria; BAF39258; BAF39258; BAD_0477.
DR   GeneID; 4556403; -.
DR   KEGG; bad:BAD_0477; -.
DR   eggNOG; ENOG4105CGM; Bacteria.
DR   eggNOG; COG1521; LUCA.
DR   HOGENOM; HOG000066025; -.
DR   KO; K03525; -.
DR   OMA; HEPWLTL; -.
DR   BioCyc; BADO367928:G1G2R-516-MONOMER; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000008702; 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; A1A0M5.
DR   SWISS-2DPAGE; A1A0M5.
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase; Metal-binding;
KW   Nucleotide-binding; Potassium; Reference proteome; Transferase.
FT   CHAIN           1..256
FT                   /note="Type III pantothenate kinase"
FT                   /id="PRO_1000214182"
FT   NP_BIND         7..14
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   REGION          108..111
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   ACT_SITE        110
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   METAL           130
FT                   /note="Monovalent cation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         133
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         185
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
SQ   SEQUENCE   256 AA;  27850 MW;  66E8C0576CFE6C65 CRC64;
     MLLMAVDIGN TNVVIGFIDD GRIAGTYRIT TKANHTSDEY GLMITQFLAL SGYKPADVDD
     VIISSVVPKV MHSFRASIVK FLDIDPMIVG PGIKTGLNIR MDNPQNMGAD CIADCAGAYY
     EYGGPILVAD FGTATTFNYV TADASVISGL ITTGIRTAAA ALWEGTAQLP EVEITRPKSI
     LAKSTKPAMQ AGLYYNFLGG IERTIAQFHK EIDEDFRVVA TGGLSRVFAD GTNMIDIYDP
     DLIFKGMWHI YDRNVR
//

If you have problems or comments...

PBIL Back to PBIL home page