ID G4QD28_TAYAM Unreviewed; 292 AA.
AC G4QD28;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
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 OrderedLocusNames=TASI_0054 {ECO:0000313|EMBL:AEP35845.1};
OS Taylorella asinigenitalis (strain MCE3).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Taylorella.
OX NCBI_TaxID=1008459 {ECO:0000313|EMBL:AEP35845.1, ECO:0000313|Proteomes:UP000009284};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MCE3;
RA Hebert L., Moumen B., Pons N., Duquesne F., Breuil M.-F., Goux D.,
RA Batto J.-M., Renault P., Laugier C., Petry S.;
RT "Genomic characterization of the Taylorella genus.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEP35845.1, ECO:0000313|Proteomes:UP000009284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCE3 {ECO:0000313|EMBL:AEP35845.1,
RC ECO:0000313|Proteomes:UP000009284};
RX PubMed=22235352; DOI=10.1371/journal.pone.0029953;
RA Hebert L., Moumen B., Pons N., Duquesne F., Breuil M.F., Goux D.,
RA Batto J.M., Laugier C., Renault P., Petry S.;
RT "Genomic characterization of the taylorella genus.";
RL PLoS ONE 7:E29953-E29953(2012).
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; CP003059; AEP35845.1; -; Genomic_DNA.
DR RefSeq; WP_014110744.1; NC_016043.1.
DR AlphaFoldDB; G4QD28; -.
DR STRING; 1008459.TASI_0054; -.
DR KEGG; tas:TASI_0054; -.
DR eggNOG; COG1521; Bacteria.
DR HOGENOM; CLU_066627_0_0_4; -.
DR OrthoDB; 9781305at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000009284; 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:UP000009284};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01274}.
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 116
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 123..126
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01274"
SQ SEQUENCE 292 AA; 32594 MW; 642D0ED9AC618FD4 CRC64;
MDKICILIDS GNSRIKARAF WLNHPEAEKN LDKAIINEIT IYNQEYAKLV GFVERITRDG
NIAKVYGVTV ATENIRTDLE NVFRSFDLEK SKDFNQKEPI VWLESEEKAF SIKNLYENTK
QLGVDRWFGI IGAHYHLTHH LKVDSNVALI HVSFGTATTV DCMHNEQLIG GTILPGLQMM
FDSLFRGTAH LPKVAVSASD IVNFPLTTHA AIQTGVVCAQ AGAVFRQIQK LWFLTTQVPY
VFISGGAKET IVDEINSICS HWSTAAGLAQ VECIELETTV LDGLQYYVSN KG
//