COAX_ALBFT
ID COAX_ALBFT Reviewed; 255 AA.
AC Q21SD6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=Rfer_3614;
OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS (Rhodoferax ferrireducens).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=338969;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-621 / DSM 15236 / T118;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL Submitted (FEB-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}.
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DR EMBL; CP000267; ABD71317.1; -; Genomic_DNA.
DR RefSeq; WP_011465880.1; NC_007908.1.
DR AlphaFoldDB; Q21SD6; -.
DR SMR; Q21SD6; -.
DR STRING; 338969.Rfer_3614; -.
DR EnsemblBacteria; ABD71317; ABD71317; Rfer_3614.
DR KEGG; rfr:Rfer_3614; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_0_0_4; -.
DR OMA; NSFIKWR; -.
DR OrthoDB; 2039419at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000008332; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004619; Type_III_PanK.
DR PANTHER; PTHR34265; PTHR34265; 1.
DR Pfam; PF03309; Pan_kinase; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00671; baf; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Potassium; Reference proteome; Transferase.
FT CHAIN 1..255
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000270897"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 7..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 103..106
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
SQ SEQUENCE 255 AA; 27174 MW; E96CA5972B122F6C CRC64;
MTFLAIDVGN TRLKWALYTH PHRDAPLLAQ GAEFLDNIDK LADGAWATLT PPTHMLGCIV
AGDAVRRRVE AQMELWDVAP QWVVASAGEA GLTNGYDYPA RLGADRWVAM IGAWHHAFST
GPARPLVVVM VGTAVTVDAI DASGKFLGGL ILPGHGIMLR ALESGTAGLH VPTGEVREFP
TNTSDALTSG GTFAIAGAVN CMVQHLRDHC GTEPKCIMAG GAGWKMAPSM SVQFELVDNL
IFDGLLEMAA RRFID
