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COAX_ROSCS
ID   COAX_ROSCS              Reviewed;         255 AA.
AC   A7NF27;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=Rcas_1296;
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Roseiflexineae;
OC   Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) 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; CP000804; ABU57393.1; -; Genomic_DNA.
DR   RefSeq; WP_012119823.1; NC_009767.1.
DR   AlphaFoldDB; A7NF27; -.
DR   SMR; A7NF27; -.
DR   STRING; 383372.Rcas_1296; -.
DR   PRIDE; A7NF27; -.
DR   EnsemblBacteria; ABU57393; ABU57393; Rcas_1296.
DR   KEGG; rca:Rcas_1296; -.
DR   eggNOG; COG1521; Bacteria.
DR   HOGENOM; CLU_066627_1_0_0; -.
DR   OMA; HEPWLTL; -.
DR   OrthoDB; 2039419at2; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000000263; 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; Transferase.
FT   CHAIN           1..255
FT                   /note="Type III pantothenate kinase"
FT                   /id="PRO_1000085859"
FT   ACT_SITE        109
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         6..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         107..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         132
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01274"
SQ   SEQUENCE   255 AA;  27502 MW;  FBD0DD74E90488F2 CRC64;
     MLLTIDIGNT NIKIGAYQGE RLTAHWRVTT ERHRLADEYL VLLHNLFDLG GIDPRHIDGC
     AISCVVPPLT GEFRALCHKY FRVDPLMVNA STPTGLQYKV DAPAELGADR IANSLAAFRR
     YGGPVIVLAF GTATTFDVIT ATGEYIGGAI APGIGISADA LFRLAAKLYQ VELVRPPKVI
     GTNTIHHMQS GVILGYAGLV EGLVRRMQAE LGTSCPVVAT GGLAELIAAE TEAITTVEPY
     LTLDGLRLIY EMNRQ
 
 
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