(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHM2_GEOS0

ID   A0A0F6BHM2_GEOS0        Unreviewed;       257 AA.
AC   A0A0F6BHM2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 23.
DE   RecName: Full=Type III pantothenate kinase {ECO:0000256|HAMAP-Rule:MF_01274};
DE            EC=2.7.1.33 {ECO:0000256|HAMAP-Rule:MF_01274};
DE   AltName: Full=PanK-III {ECO:0000256|HAMAP-Rule:MF_01274};
DE   AltName: Full=Pantothenic acid kinase {ECO:0000256|HAMAP-Rule:MF_01274};
GN   Name=coaX {ECO:0000256|HAMAP-Rule:MF_01274};
GN   OrderedLocusNames=GY4MC1_0067 {ECO:0000313|EMBL:ADP72923.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72923.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72923.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72923.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC       first step in CoA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01274,
CC       ECO:0000256|SAAS:SAAS00088441}.
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:0000256|HAMAP-
CC         Rule:MF_01274, ECO:0000256|SAAS:SAAS01124593};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|SAAS:SAAS00611758};
CC   -!- COFACTOR:
CC       Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01274};
CC       Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01274};
CC       Note=A monovalent cation. Ammonium or potassium.
CC       {ECO:0000256|HAMAP-Rule:MF_01274};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC       (R)-pantothenate: step 1/5. {ECO:0000256|HAMAP-Rule:MF_01274,
CC       ECO:0000256|SAAS:SAAS00088429}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274,
CC       ECO:0000256|SAAS:SAAS00701620}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
CC       ECO:0000256|SAAS:SAAS00088436}.
CC   -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00701623}.
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DR   EMBL; CP002293; ADP72923.1; -; Genomic_DNA.
DR   RefSeq; WP_003247473.1; NC_014650.1.
DR   EnsemblBacteria; ADP72923; ADP72923; GY4MC1_0067.
DR   GeneID; 29237311; -.
DR   KEGG; gmc:GY4MC1_0067; -.
DR   KO; K03525; -.
DR   OMA; HEPWLTL; -.
DR   OrthoDB; 2039419at2; -.
DR   BioCyc; GSP581103:G1GOQ-80-MONOMER; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000002034; 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; A0A0F6BHM2.
DR   SWISS-2DPAGE; A0A0F6BHM2.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461390};
KW   Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461336};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461333};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461374};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01274};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461342};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00173372};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461385, ECO:0000313|EMBL:ADP72923.1}.
FT   NP_BIND       6     13       ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
FT   REGION      107    110       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01274}.
FT   ACT_SITE    109    109       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
FT   METAL       129    129       Monovalent cation. {ECO:0000256|HAMAP-
FT                                Rule:MF_01274}.
FT   BINDING     100    100       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
FT   BINDING     132    132       ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
FT   BINDING     184    184       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
SQ   SEQUENCE   257 AA;  27971 MW;  D2125D5279BF5AA6 CRC64;
     MIFVLDVGNT NTVLGVYDGD ELKHHWRIET SRGKTEDEYG MLIKALLNHV GLQFSDIDGI
     IISSVVPPIM FALERMCLKY FHIKPIIVGP GIKTGLDIKY DNPREVGADR IVNAVAGIHL
     YGSPLIIVDF GTATTYCYIN EHKQYMGGAI APGIMISTEA LFARAAKLPR IEIARPDDII
     GKNTVSAMQA GILYGYVGQV EGIVARMKAK SPVPPKVIAT GGLASLIASE SDVIDIVDPF
     LTLTGLKILY EKNVDKK
//

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