(data stored in SCRATCH 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   11-DEC-2019, entry version 27.
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;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72923.1};
RN   [1] {ECO:0000313|EMBL:ADP72923.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72923.1};
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., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   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, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29032, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC         EC=2.7.1.33; Evidence={ECO:0000256|HAMAP-Rule:MF_01274,
CC         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;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01274};
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01274};
CC       Note=A monovalent cation. Ammonium or potassium. {ECO:0000256|HAMAP-
CC       Rule:MF_01274};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       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   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   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00461333};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01274, 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, 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
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   REGION          107..110
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   ACT_SITE        109
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   METAL           129
FT                   /note="Monovalent cation"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   BINDING         100
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   BINDING         132
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   BINDING         184
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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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