COAX_MAGMM
ID COAX_MAGMM Reviewed; 255 AA.
AC A0L7P3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Mmc1_1477;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(2009).
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; CP000471; ABK43986.1; -; Genomic_DNA.
DR RefSeq; WP_011713139.1; NC_008576.1.
DR AlphaFoldDB; A0L7P3; -.
DR SMR; A0L7P3; -.
DR STRING; 156889.Mmc1_1477; -.
DR EnsemblBacteria; ABK43986; ABK43986; Mmc1_1477.
DR KEGG; mgm:Mmc1_1477; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_1_0_5; -.
DR OMA; HEPWLTL; -.
DR OrthoDB; 2039419at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000002586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome; Transferase.
FT CHAIN 1..255
FT /note="Type III pantothenate kinase"
FT /id="PRO_1000054386"
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 129
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
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; 27488 MW; 5C6DA4D214D8BCEB CRC64;
MLLVMDVGNT NIVLGLYEGD QLAHSWRIAS RIERTGDEYG ILLANLLQLK QVDAHGINGV
ILASVVPPIG SALVRAVRRY LGLETLVVGA SMKYGLPLSE ESPSGVGADR LVNAVAVFDK
VAHAAIVVDF GTATTFDLIG EQGIYLGGAI APGLNSSLDA LFEKTAKLPR IELFHPERVI
GKTTEEAMRS GLYWGYVGLV DGIIERMRVE SGFANIHVTA TGGLAKLIAR DSRCIDDVDD
MLTLTGLRLL YQRNR
