ID   A0A926M4X8_9PROT        Unreviewed;       248 AA.
AC   A0A926M4X8;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   03-MAY-2023, entry version 2.
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   ORFNames=IDH22_00375 {ECO:0000313|EMBL:MBD1142419.1};
OS   Pelagibacterales bacterium SAG-MED35.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Pelagibacterales.
OX   NCBI_TaxID=2760037 {ECO:0000313|EMBL:MBD1142419.1, ECO:0000313|Proteomes:UP000611396};
RN   [1] {ECO:0000313|EMBL:MBD1142419.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SAG-MED35 {ECO:0000313|EMBL:MBD1142419.1};
RX   PubMed=31840364;
RA   Haro-Moreno J.M., Rodriguez-Valera F., Rosselli R., Martinez-Hernandez F.,
RA   Roda-Garcia J.J., Gomez M.L., Fornas O., Martinez-Garcia M.,
RA   Lopez-Perez M.;
RT   "Ecogenomics of the SAR11 clade.";
RL   Environ. Microbiol. 22:1748-1763(2020).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC       first step in CoA biosynthesis. {ECO:0000256|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:0000256|ARBA:ARBA00001206,
CC         ECO:0000256|HAMAP-Rule:MF_01274};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000256|ARBA:ARBA00001958};
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|ARBA:ARBA00005225,
CC       ECO:0000256|HAMAP-Rule:MF_01274}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274}.
CC   -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01274}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01274}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBD1142419.1}.
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DR   EMBL; JACWEF010000001; MBD1142419.1; -; Genomic_DNA.
DR   Proteomes; UP000611396; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR004619; Type_III_PanK.
DR   PANTHER; PTHR34265; TYPE III PANTOTHENATE KINASE; 1.
DR   PANTHER; PTHR34265:SF1; TYPE III PANTOTHENATE KINASE; 1.
DR   Pfam; PF03309; Pan_kinase; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01274};
KW   Coenzyme A biosynthesis {ECO:0000256|ARBA:ARBA00022993, ECO:0000256|HAMAP-
KW   Rule:MF_01274};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01274};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000313|EMBL:MBD1142419.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01274};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01274};
KW   Potassium {ECO:0000256|HAMAP-Rule:MF_01274};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01274}.
FT   ACT_SITE        105
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   BINDING         6..13
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   BINDING         103..106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   BINDING         124
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   BINDING         127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT   BINDING         178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
SQ   SEQUENCE   248 AA;  28149 MW;  C11A6ED9DE7F66DF CRC64;
     MYILGDIGNT ETKIWLVSKK NHIIKKINFS SKEVTNYKLS KIFKKYNFKF KDIEKILFCS
     VVPPTFNLIK KFLSKKTNIK CREVKSLSLK SLIKIKVDYK QVGSDRITNA ISLMNNKNNF
     IILDFGTATT FDVLVQNTYY GGIIAPGLKL SLNSLSDKAT LIPKINLKKI TKVIGNNTIS
     AVRSGFFWGY AGLIDNIIYL IKKETRKTFK VIITGGFSDL FKNSIKTKVS QNQDITIKGL
     IKISRLIK
//