ID A0A0R2K7N6_9LACO Unreviewed; 307 AA.
AC A0A0R2K7N6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=IV43_GL001481 {ECO:0000313|EMBL:KRN83349.1}, LAC1533_1805
GN {ECO:0000313|EMBL:SFV41228.1};
OS Ligilactobacillus acidipiscis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=89059 {ECO:0000313|EMBL:KRN83349.1, ECO:0000313|Proteomes:UP000051491};
RN [1] {ECO:0000313|EMBL:KRN83349.1, ECO:0000313|Proteomes:UP000051491}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15353 {ECO:0000313|EMBL:KRN83349.1,
RC ECO:0000313|Proteomes:UP000051491};
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).
RN [2] {ECO:0000313|EMBL:SFV41228.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACA-DC 1533 {ECO:0000313|EMBL:SFV41228.1};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000190935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACA-DC 1533 {ECO:0000313|Proteomes:UP000190935};
RA Papadimitriou K.;
RL Submitted (NOV-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; JQBK01000043; KRN83349.1; -; Genomic_DNA.
DR EMBL; LT630287; SFV41228.1; -; Genomic_DNA.
DR RefSeq; WP_056988104.1; NZ_LT630287.1.
DR AlphaFoldDB; A0A0R2K7N6; -.
DR STRING; 89059.LAC1533_1805; -.
DR KEGG; laca:LAC1533_1805; -.
DR PATRIC; fig|89059.3.peg.1582; -.
DR OrthoDB; 1550976at2; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000051491; Unassembled WGS sequence.
DR Proteomes; UP000190935; Chromosome i.
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:KRN83349.1};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00215};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00215, ECO:0000313|EMBL:SFV41228.1}.
FT DOMAIN 85..231
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; 36172 MW; 2BD1932810C07560 CRC64;
MENRLNYYQI PREEWRSFYR DHYVPLSSRE LMRIKSLNDE ISLKDVEEIY MPLVHLLGMR
MEARNYGQNQ LADFLGIKHK PTPFILGIAG SVAVGKSTVA RLLRDLLTEI FPNKKIQQIT
TDGFLYPSEE LKKRHIMKRK GFPESYDMKA LINFINDVKN GLPAKAPVYS HQVYDRVKGE
YDLIDQPDVL ILEGINVLQL PSNQQIFVSD FFDFSIYVDA DEKLIKKWYM ERFELILDRA
QDEPNDYYHA YAIGDRDVAR KMAENVWHDV NHKNLHSYIL PTRNRADLVL NKGENHLVDE
LYLRKFV
//
