ID D5E4L7_MYCCM Unreviewed; 258 AA.
AC D5E4L7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 74.
DE RecName: Full=Type III pantothenate kinase {ECO:0000256|ARBA:ARBA00040883, ECO:0000256|HAMAP-Rule:MF_01274};
DE EC=2.7.1.33 {ECO:0000256|ARBA:ARBA00012102, 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=panK {ECO:0000313|EMBL:ADE19736.1};
GN Synonyms=coaX {ECO:0000256|HAMAP-Rule:MF_01274};
GN OrderedLocusNames=MCRO_0026 {ECO:0000313|EMBL:ADE19736.1};
OS Mycoplasma crocodyli (strain ATCC 51981 / MP145).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=512564 {ECO:0000313|EMBL:ADE19736.1, ECO:0000313|Proteomes:UP000001845};
RN [1] {ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RA Glass J.I., Durkin A.S., Hostetler J., Jackson J., Johnson J., May M.A.,
RA Paralanov V., Radune D., Szczypinski B., Brown D.R.;
RT "The complete genome of Mycoplasma crocodyli MP145.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MP145;
RA Ma Z., Wang X., Liu H.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADE19736.1, ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RX PubMed=21460083; DOI=10.1128/JB.00309-11;
RA Brown D.R., Farmerie W.G., May M., Benders G.A., Durkin A.S., Hlavinka K.,
RA Hostetler J., Jackson J., Johnson J., Miller R.H., Paralanov V., Radune D.,
RA Szczypinski B., Glass J.I.;
RT "Genome sequences of Mycoplasma alligatoris A21JP2T and Mycoplasma
RT crocodyli MP145T.";
RL J. Bacteriol. 193:2892-2893(2011).
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|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01274}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01274}.
CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC {ECO:0000256|ARBA:ARBA00038036, 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}.
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DR EMBL; CP001991; ADE19736.1; -; Genomic_DNA.
DR RefSeq; WP_013054512.1; NC_014014.1.
DR AlphaFoldDB; D5E4L7; -.
DR STRING; 512564.MCRO_0026; -.
DR KEGG; mcd:MCRO_0026; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_1089146_0_0_14; -.
DR OMA; IVANAYY; -.
DR OrthoDB; 397644at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000001845; 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 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 NCBIfam; TIGR00671; baf; 1.
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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW 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|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01274};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01274};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_01274};
KW Reference proteome {ECO:0000313|Proteomes:UP000001845};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01274}.
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 17..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 112..115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
SQ SEQUENCE 258 AA; 28873 MW; A13B569A533B6D10 CRC64;
MISKNFKTNI KSYLTIDIGN SFIKMGLFNE NKELIDFSMF PSKKIDLDKI ISKLETYKMK
NIVSVIMGCV VKSYWEKLNL VLKNVLSIEA YRINEKTKFS FDSSGFIAKG IGDDLLALSE
YAVRKNENSI AFSFGTSNVG LFIVDKKLIG VSISAGLESS YNSLISKASL LKKTKIDRAS
LLSYGQDTSG ALESGYFHHR NGFLLSFVNS IKAKYDDKNF YIVASGNAAT SFNNNHFVEI
NKYAILEGYL NILTINIK
//