ID A0A0R2DS53_9LACO Unreviewed; 307 AA.
AC A0A0R2DS53;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=FD13_GL000949 {ECO:0000313|EMBL:KRN03194.1};
OS Levilactobacillus senmaizukei DSM 21775 = NBRC 103853.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1423803 {ECO:0000313|EMBL:KRN03194.1, ECO:0000313|Proteomes:UP000051589};
RN [1] {ECO:0000313|EMBL:KRN03194.1, ECO:0000313|Proteomes:UP000051589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21775 {ECO:0000313|EMBL:KRN03194.1,
RC ECO:0000313|Proteomes:UP000051589};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRN03194.1}.
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DR EMBL; AYZH01000002; KRN03194.1; -; Genomic_DNA.
DR RefSeq; WP_061777039.1; NZ_BCWD01000018.1.
DR AlphaFoldDB; A0A0R2DS53; -.
DR STRING; 1423803.FD13_GL000949; -.
DR PATRIC; fig|1423803.3.peg.948; -.
DR OrthoDB; 1550976at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000051589; 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:KRN03194.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00215}.
FT DOMAIN 85..229
FT /note="Phosphoribulokinase/uridine kinase"
FT /evidence="ECO:0000259|Pfam:PF00485"
FT BINDING 90..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00215"
SQ SEQUENCE 307 AA; 35767 MW; F2BA3F5E1E830D03 CRC64;
MSDPINYNAF TRAEWRAFSD DAKLPLTQES LRQIKAFNDR ISLQDVQDIY IPLIHLLRLQ
FNHYRLLQQD KATFLQQPAH RVPFIIGIAG SVAVGKSTAA RLLEVLLNHY FKNSNIQLIT
TDGFLYPNDE LKRRQLMSRK GFPESYDMAA LIQFLNDVKA GVPSIKAPLY SHKIYDIVPD
EFETITAPDI LIVEGINTLQ LPTNEQIYVS DFTDFSIYVD AEANLIEDWF LERFELLLET
AFRDPENYYY PYAIGDRDEA MAKGKKVWED IDLKNLEEYI LPTRNRADMI IHKTIGHRID
RLLLRKY
//
