(data stored in ACNUC7421 zone)

SWISSPROT: D6XV60_BACIE

ID   D6XV60_BACIE            Unreviewed;       255 AA.
AC   D6XV60;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
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=Bsel_0067 {ECO:0000313|EMBL:ADH97618.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97618.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97618.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01274}.
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DR   EMBL; CP001791; ADH97618.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0067; -.
DR   EnsemblBacteria; ADH97618; ADH97618; Bsel_0067.
DR   KEGG; bse:Bsel_0067; -.
DR   eggNOG; ENOG4107QNB; Bacteria.
DR   eggNOG; COG1521; LUCA.
DR   HOGENOM; HOG000066025; -.
DR   KO; K03525; -.
DR   OMA; HEPWLTL; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000000271; 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; D6XV60.
DR   SWISS-2DPAGE; D6XV60.
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:UP000000271};
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   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01274,
KW   ECO:0000256|SAAS:SAAS00461385}.
FT   NP_BIND       8     15       ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
FT   REGION      109    112       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01274}.
FT   ACT_SITE    111    111       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
FT   METAL       131    131       Monovalent cation. {ECO:0000256|HAMAP-
FT                                Rule:MF_01274}.
FT   BINDING     134    134       ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
FT   BINDING     186    186       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01274}.
SQ   SEQUENCE   255 AA;  27968 MW;  02CD30AB7CA6E53D CRC64;
     MLMKLVMDIG NTTISIGLYK KQTRIAEWTV QTDYEKTVDE YGVLLGQLFM MNNLLTSEVK
     RIMVSSVVPP LDETIRQVCA RYLAIEPVFV GPGVKTGLNI STENPREVGS DRIVNAVAAL
     EHYTPPLIVV DFGTATTVCY VNAKRQYVGG VIAPGMSIAM DALYDKASKL PKIDLTATDS
     VIGRNTTDAM RSGYLYGYLG QMEGIVQRMK DEQGEATVVA TGDHAVILGE HSRLIDHVHP
     HLTLDGLAIL DERQP
//

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