ID A0A0L0KKP8_9ACTN Unreviewed; 265 AA.
AC A0A0L0KKP8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=coaX {ECO:0000256|HAMAP-Rule:MF_01274,
GN ECO:0000313|EMBL:GAQ54777.1};
GN ORFNames=a10_04592 {ECO:0000313|EMBL:GAQ54777.1}, IQ63_08615
GN {ECO:0000313|EMBL:KND38408.1}, Saa2_01012
GN {ECO:0000313|EMBL:GAV38133.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND38408.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|EMBL:KND38408.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCPPB 4445 {ECO:0000313|EMBL:KND38408.1};
RA Chen X.-L., Norrbom A., Zhu C.-D.;
RT "A systematic study of Ichneumonosoma Meijere, Pelmatops Enderlein,
RT Pseudopelmatops Shiraki and Soita Walker (Diptera: Tephritidae).";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000058287, ECO:0000313|Proteomes:UP000186713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=a10 {ECO:0000313|Proteomes:UP000058287}, A2
RC {ECO:0000313|EMBL:GAV38133.1}, and a2
RC {ECO:0000313|Proteomes:UP000186713};
RG Cross-ministerial Strategic Innovation Promotion Program (SIP) consortium;
RA Tomihama T., Ikenaga M., Sakai M., Okubo T., Ikeda S.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:GAQ54777.1, ECO:0000313|Proteomes:UP000058287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=a10 {ECO:0000313|Proteomes:UP000058287}, and A10
RC {ECO:0000313|EMBL:GAQ54777.1};
RA Tomihama T., Nishi Y., Sakai M., Ikenaga M., Okubo T., Ikeda S.;
RT "Draft Genome Sequences of Streptomyces scabiei S58, Streptomyces
RT turgidiscabies T45, and Streptomyces acidiscabies a10, the Pathogens of
RT Potato Common Scab, Isolated in Japan.";
RL Genome Announc. 4:e00062-16(2016).
RN [5] {ECO:0000313|Proteomes:UP000058287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=a10 {ECO:0000313|Proteomes:UP000058287}, a2
RC {ECO:0000313|Proteomes:UP000186713}, and A2
RC {ECO:0000313|EMBL:GAV38133.1};
RA Tomihama T., Ikenaga M., Sakai M., Okubo T., Ikeda S.;
RT "Draft genome of pathogenic Streptomyces sp. in Japan.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KND38408.1}.
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DR EMBL; BCMK01000037; GAQ54777.1; -; Genomic_DNA.
DR EMBL; BCML01000005; GAV38133.1; -; Genomic_DNA.
DR EMBL; JPPY01000046; KND38408.1; -; Genomic_DNA.
DR RefSeq; WP_010351467.1; NZ_PCGS01000668.1.
DR AlphaFoldDB; A0A0L0KKP8; -.
DR STRING; 42234.IQ63_08615; -.
DR GeneID; 33086273; -.
DR PATRIC; fig|42234.21.peg.1780; -.
DR eggNOG; COG1521; Bacteria.
DR OrthoDB; 9804707at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000037151; Unassembled WGS sequence.
DR Proteomes; UP000058287; Unassembled WGS sequence.
DR Proteomes; UP000186713; Unassembled WGS sequence.
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 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 Metal-binding {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:UP000037151};
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 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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 134
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
SQ SEQUENCE 265 AA; 28202 MW; 6D75B9118F06B471 CRC64;
MLLTIDVGNT HTTLGLFDGE EIVEHWRIST DARRTADELA VLLQGLMGMH PLLGDELGDG
IDGIAICATV PSVLHELREV TRRYYGDVPA VLVEPGVKTG VPILTDNPKE VGADRIINAV
AAVELYGGPA VVVDFGTATT FDAVSARGEY VGGVIAPGIE ISVEALGVRG AQLRKIEVAR
PRSVIGKNTV EAMQSGIVYG FAGQVDGVVQ RMIRELATDP EDVTVIATGG LAPMVLGEAS
VIDEHEPWLT LIGLRLVYER NVSRM
//
