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Database: UniProt
Entry: D5E4L7_MYCCM
LinkDB: D5E4L7_MYCCM
Original site: D5E4L7_MYCCM 
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
//
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