(data stored in ACNUC1104 zone)
SWISSPROT: D5USE2_TSUPD
ID D5USE2_TSUPD Unreviewed; 285 AA.
AC D5USE2;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 08-MAY-2019, entry version 53.
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 OrderedLocusNames=Tpau_0569 {ECO:0000313|EMBL:ADG77209.1};
OS Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 /
OS NBRC 16120 / NCTC 13040) (Corynebacterium paurometabolum).
OC Bacteria; Actinobacteria; Corynebacteriales; Tsukamurellaceae;
OC Tsukamurella.
OX NCBI_TaxID=521096 {ECO:0000313|EMBL:ADG77209.1, ECO:0000313|Proteomes:UP000001213};
RN [1] {ECO:0000313|Proteomes:UP000001213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC {ECO:0000313|Proteomes:UP000001213};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA Ivanova N., Mikhailova N., Munk A.C., Brettin T., Detter J.C.,
RA Tapia R., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Tsukamurella paurometabola DSM 20162.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADG77209.1, ECO:0000313|Proteomes:UP000001213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040
RC {ECO:0000313|Proteomes:UP000001213};
RX PubMed=21886861;
RA Munk A.C., Lapidus A., Lucas S., Nolan M., Tice H., Cheng J.F.,
RA Del Rio T.G., Goodwin L., Pitluck S., Liolios K., Huntemann M.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Tapia R., Han C., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Brettin T., Yasawong M., Brambilla E.M., Rohde M.,
RA Sikorski J., Goker M., Detter J.C., Woyke T., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Tsukamurella paurometabola type strain
RT (no. 33).";
RL Stand. Genomic Sci. 4:342-351(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01274,
CC ECO:0000256|SAAS:SAAS00088441}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP
CC + H(+); Xref=Rhea:RHEA:16373, ChEBI:CHEBI:10986,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; EC=2.7.1.33; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01274, ECO:0000256|SAAS:SAAS01124593};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|SAAS:SAAS00611758};
CC -!- COFACTOR:
CC Name=NH4(+); Xref=ChEBI:CHEBI:28938; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01274};
CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01274};
CC Note=A monovalent cation. Ammonium or potassium.
CC {ECO:0000256|HAMAP-Rule:MF_01274};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from
CC (R)-pantothenate: step 1/5. {ECO:0000256|HAMAP-Rule:MF_01274,
CC ECO:0000256|SAAS:SAAS00088429}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01274,
CC ECO:0000256|SAAS:SAAS00701620}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
CC ECO:0000256|SAAS:SAAS00088436}.
CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_01274, ECO:0000256|SAAS:SAAS00701623}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01274}.
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DR EMBL; CP001966; ADG77209.1; -; Genomic_DNA.
DR RefSeq; WP_013125251.1; NC_014158.1.
DR STRING; 521096.Tpau_0569; -.
DR EnsemblBacteria; ADG77209; ADG77209; Tpau_0569.
DR KEGG; tpr:Tpau_0569; -.
DR eggNOG; ENOG4105CGM; Bacteria.
DR eggNOG; COG1521; LUCA.
DR HOGENOM; HOG000066025; -.
DR KO; K03525; -.
DR OMA; HEPWLTL; -.
DR OrthoDB; 2039419at2; -.
DR BioCyc; TPAU521096:G1GKO-552-MONOMER; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000001213; 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 HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR InterPro; IPR004619; Type_III_PanK.
DR PANTHER; PTHR34265; PTHR34265; 1.
DR Pfam; PF03309; Pan_kinase; 1.
DR TIGRFAMs; TIGR00671; baf; 1.
PE 3: Inferred from homology;
DR PRODOM; D5USE2.
DR SWISS-2DPAGE; D5USE2.
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01274,
KW ECO:0000256|SAAS:SAAS00461390};
KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_01274,
KW ECO:0000256|SAAS:SAAS00461336};
KW Complete proteome {ECO:0000313|Proteomes:UP000001213};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01274,
KW ECO:0000256|SAAS:SAAS00461333};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01274,
KW ECO:0000256|SAAS:SAAS00461374};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01274};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01274,
KW ECO:0000256|SAAS:SAAS00461342};
KW Potassium {ECO:0000256|HAMAP-Rule:MF_01274,
KW ECO:0000256|SAAS:SAAS00173372};
KW Reference proteome {ECO:0000313|Proteomes:UP000001213};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01274,
KW ECO:0000256|SAAS:SAAS00461385}.
FT NP_BIND 6 13 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
FT REGION 118 121 Substrate binding. {ECO:0000256|HAMAP-
FT Rule:MF_01274}.
FT ACT_SITE 120 120 Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT MF_01274}.
FT METAL 144 144 Monovalent cation. {ECO:0000256|HAMAP-
FT Rule:MF_01274}.
FT BINDING 147 147 ATP. {ECO:0000256|HAMAP-Rule:MF_01274}.
FT BINDING 199 199 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_01274}.
SQ SEQUENCE 285 AA; 29611 MW; 505660BEC4ABA082 CRC64;
MLLAIDAGNT SVTVGLFAAG TDGGAGELLG TWRLRSDPRM TSDELALVIR GFLTGPGTEP
GFDPAAVTGV TALSTVPELL RSLRAMAPRY YPGAQHVILE PGVKTGVPLH VDNPREVGTD
RVANAAGAFE VCGRSAGTPC IVVDFGTSTR VDVVSAKGEF LGGAIAPGVG SALDALAERT
VALRRVELVP PRSVVGKNTV EALQSGIIYG FAGLVDALVR RALETVPDAR VIATGGYDDG
VAAECATITD RRADLTLQGL RAVYLREIAS RATRAERKAH PRDSV
//
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