ID A0A0S9DV33_9MICO Unreviewed; 318 AA.
AC A0A0S9DV33;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Pantothenate kinase {ECO:0000256|ARBA:ARBA00015080, ECO:0000256|HAMAP-Rule:MF_00215};
DE EC=2.7.1.33 {ECO:0000256|ARBA:ARBA00012102, ECO:0000256|HAMAP-Rule:MF_00215};
DE AltName: Full=Pantothenic acid kinase {ECO:0000256|HAMAP-Rule:MF_00215};
GN Name=coaA {ECO:0000256|HAMAP-Rule:MF_00215};
GN ORFNames=ASF06_05795 {ECO:0000313|EMBL:KQO09766.1};
OS Agreia sp. Leaf244.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agreia.
OX NCBI_TaxID=1736305 {ECO:0000313|EMBL:KQO09766.1, ECO:0000313|Proteomes:UP000051484};
RN [1] {ECO:0000313|EMBL:KQO09766.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO09766.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO09766.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf244 {ECO:0000313|EMBL:KQO09766.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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_00215, ECO:0000256|RuleBase:RU003530};
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_00215, ECO:0000256|RuleBase:RU003530}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530}.
CC -!- SIMILARITY: Belongs to the prokaryotic pantothenate kinase family.
CC {ECO:0000256|ARBA:ARBA00006087, ECO:0000256|HAMAP-Rule:MF_00215,
CC ECO:0000256|RuleBase:RU003530}.
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:KQO09766.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMLX01000002; KQO09766.1; -; Genomic_DNA.
DR RefSeq; WP_055944614.1; NZ_LMLX01000002.1.
DR AlphaFoldDB; A0A0S9DV33; -.
DR STRING; 1736305.ASF06_05795; -.
DR OrthoDB; 1550976at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000051484; 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: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 CDD; cd02025; PanK; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00215; Pantothen_kinase_1; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004566; PanK.
DR InterPro; IPR006083; PRK/URK.
DR NCBIfam; TIGR00554; panK_bact; 1.
DR PANTHER; PTHR10285:SF139; PANTOTHENATE KINASE; 1.
DR PANTHER; PTHR10285; URIDINE KINASE; 1.
DR Pfam; PF00485; PRK; 1.
DR PIRSF; PIRSF000545; Pantothenate_kin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW Coenzyme A biosynthesis {ECO:0000256|HAMAP-Rule:MF_00215,
KW ECO:0000256|RuleBase:RU003530};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000256|RuleBase:RU003530};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000313|EMBL:KQO09766.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00215}.
FT DOMAIN 95..233
FT /note="Phosphoribulokinase/uridine kinase"
FT /evidence="ECO:0000259|Pfam:PF00485"
FT BINDING 100..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00215"
SQ SEQUENCE 318 AA; 35293 MW; B7A968F60FDEB687 CRC64;
MTDIGHAPHS TGHPTPFREI DRGDWAALAP STPQPLSETE IVQLRGLGEP LDMTEVAEVY
LPLSRLLNLY AAGAKRLHAS TSDYLGDRQT ATPFVIGVAG SVAVGKSTIA RLLRELLARW
SDTPRVELVA TDGFLYPNAE LTRRGIMHRK GFPESYDRRA LLRFISAVKS GVPEVRAPFY
SHLAYDIVPE AQIVVRQPDI LIVEGLNVLQ PPLPGQGLAV SDLFDFSIYV DARTSDIATW
YVDRFLALKR GAFANPNSFF HRYAQLSDDD ARSTAAEIWR SINEPNLVEN IQPTKSRATL
VLRKSSTHAV DRVLLRKI
//
