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Database: UniProt
Entry: L0MBF0_9GAMM
LinkDB: L0MBF0_9GAMM
Original site: L0MBF0_9GAMM 
ID   L0MBF0_9GAMM            Unreviewed;       316 AA.
AC   L0MBF0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 70.
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=D781_0241 {ECO:0000313|EMBL:AGB80622.1};
OS   Serratia sp. FGI94.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=671990 {ECO:0000313|EMBL:AGB80622.1, ECO:0000313|Proteomes:UP000011001};
RN   [1] {ECO:0000313|EMBL:AGB80622.1, ECO:0000313|Proteomes:UP000011001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGI94 {ECO:0000313|EMBL:AGB80622.1,
RC   ECO:0000313|Proteomes:UP000011001};
RX   PubMed=23516234;
RA   Aylward F.O., Tremmel D.M., Starrett G.J., Bruce D.C., Chain P., Chen A.,
RA   Davenport K.W., Detter C., Han C.S., Han J., Huntemann M., Ivanova N.N.,
RA   Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M., Pagani I., Pati A.,
RA   Pitluck S., Teshima H., Deshpande S., Goodwin L., Woyke T., Currie C.R.;
RT   "Complete Genome of Serratia sp. Strain FGI 94, a Strain Associated with
RT   Leaf-Cutter Ant Fungus Gardens.";
RL   Genome Announc. 1:E0023912-E0023912(2013).
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; CP003942; AGB80622.1; -; Genomic_DNA.
DR   RefSeq; WP_015344218.1; NC_020064.1.
DR   AlphaFoldDB; L0MBF0; -.
DR   GeneID; 61763769; -.
DR   KEGG; smaf:D781_0241; -.
DR   PATRIC; fig|1249634.3.peg.219; -.
DR   eggNOG; COG1072; Bacteria.
DR   HOGENOM; CLU_053818_1_1_6; -.
DR   OrthoDB; 1550976at2; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000011001; 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   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:AGB80622.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00215}.
FT   DOMAIN          90..244
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
FT   BINDING         95..102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00215"
SQ   SEQUENCE   316 AA;  35868 MW;  76BFC253B7E6A48D CRC64;
     MIKREQSLAT PYLQFDRTQW AALRDSVPLT LSEEEIVKLK GINEDLSLEE VAQIYLPLSR
     LLNFYISSNL RRQAVLEQFL GTDGQKIPYV IGIAGSVAVG KSTTARLLQA LLSSWPEHRS
     VELVTTDGFL HPNKVLNERG LMKKKGFPQS YDMHSLVKFV SEVKSGAKRV TAPVYSHLIY
     DVVPDGNKVI EQPDILILEG LNVLQSGMDY PHDPHHVFVS DFVDFSIYVD ASAELLQTWY
     INRFLKFRQG AFSNPDSYFH NYAKLSESEA VKIATQLWNE INGLNLQQNI LPTRERASLI
     MTKSANHAVE HVRLRK
//
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