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Entry: A0A1I6KUQ5_9MICO
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ID   A0A1I6KUQ5_9MICO        Unreviewed;       321 AA.
AC   A0A1I6KUQ5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=SAMN04487846_1000 {ECO:0000313|EMBL:SFR94670.1};
OS   Microbacterium sp. cf046.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1761803 {ECO:0000313|EMBL:SFR94670.1, ECO:0000313|Proteomes:UP000199422};
RN   [1] {ECO:0000313|EMBL:SFR94670.1, ECO:0000313|Proteomes:UP000199422}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF046 {ECO:0000313|EMBL:SFR94670.1,
RC   ECO:0000313|Proteomes:UP000199422};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FOZJ01000001; SFR94670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6KUQ5; -.
DR   STRING; 1761803.SAMN04487846_1000; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000199422; 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:SFR94670.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199422};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00215}.
FT   DOMAIN          98..248
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   BINDING         103..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   321 AA;  35876 MW;  F74B16F834491542 CRC64;
     MFGMPADDAA TTVTPSLSLY REIDRGEWAR LAADMAQPLS ETEIVQIRGL GDMLDMAEVR
     EVYLPLSRLL SLYANATKRL GADTSAFLRE PDTTTPFVVA VAGSVAVGKS TIARLLRELM
     SRWPGTPRVE LITTDGFLYP NAELERRGLM DRKGFPESYD RRAMVRFLTD VKSGAPEARA
     PFYSHMRYDI VPDAHITVRR PDVVIVEGLN VLQPSPSPSD MAVSELFDFS IYVDAQTDHI
     AAWYVDRFLA LRRGAFANPS SFFNVFAHLT DEEAVQTAMG YWNEINLPNL RENVLPTKHQ
     ATLILDKAAS HSVARVLLRK L
//
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