ID   PANK3_BOVIN             Reviewed;         370 AA.
AC   Q08DA5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Pantothenate kinase 3;
DE            EC=2.7.1.33 {ECO:0000250|UniProtKB:Q9H999};
DE   AltName: Full=Pantothenic acid kinase 3;
GN   Name=PANK3;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Basal ganglia;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of pantothenate to generate 4'-
CC       phosphopantothenate in the first and rate-determining step of coenzyme
CC       A (CoA) synthesis. {ECO:0000250|UniProtKB:Q9H999}.
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:0000250|UniProtKB:Q9H999};
CC   -!- ACTIVITY REGULATION: Subject to allosteric regulation, exists in two
CC       distinct conformational states, a catalytically incompetent (or open)
CC       conformation stabilized by the binding of acetyl(acyl)-CoA, and a
CC       catalytically competent (or closed) conformation stabilized by ATP-
CC       binding. Inhibited by acetyl-CoA and its thioesters which act as
CC       allosteric inhibitors and compete with the ATP-binding site.
CC       {ECO:0000250|UniProtKB:Q9H999}.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5. {ECO:0000250|UniProtKB:Q9H999}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9H999}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC       {ECO:0000305}.
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DR   EMBL; BC123859; AAI23860.1; -; mRNA.
DR   RefSeq; NP_001068931.1; NM_001075463.1.
DR   AlphaFoldDB; Q08DA5; -.
DR   SMR; Q08DA5; -.
DR   STRING; 9913.ENSBTAP00000015780; -.
DR   PaxDb; Q08DA5; -.
DR   PRIDE; Q08DA5; -.
DR   Ensembl; ENSBTAT00000015780; ENSBTAP00000015780; ENSBTAG00000011895.
DR   GeneID; 510749; -.
DR   KEGG; bta:510749; -.
DR   CTD; 79646; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011895; -.
DR   VGNC; VGNC:32565; PANK3.
DR   eggNOG; KOG2201; Eukaryota.
DR   GeneTree; ENSGT00940000156396; -.
DR   HOGENOM; CLU_011154_0_1_1; -.
DR   InParanoid; Q08DA5; -.
DR   OMA; WAQEGDN; -.
DR   OrthoDB; 865329at2759; -.
DR   TreeFam; TF314866; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000009136; Chromosome 20.
DR   Bgee; ENSBTAG00000011895; Expressed in liver and 112 other tissues.
DR   ExpressionAtlas; Q08DA5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1905502; F:acetyl-CoA binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004594; F:pantothenate kinase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0019842; F:vitamin binding; ISS:UniProtKB.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR004567; Type_II_PanK.
DR   PANTHER; PTHR12280; PTHR12280; 1.
DR   Pfam; PF03630; Fumble; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR00555; panK_eukar; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..370
FT                   /note="Pantothenate kinase 3"
FT                   /id="PRO_0000261356"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H999"
FT   BINDING         192
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H999"
FT   BINDING         195
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H999"
FT   BINDING         207
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H999"
SQ   SEQUENCE   370 AA;  41117 MW;  E8EEE55E678DB23A CRC64;
     MKIKDAKKPS FPWFGMDIGG TLVKLSYFEP IDITAEEEQE EVESLKSIRK YLTSNVAYGS
     TGIRDVHLEL KDLTLFGRRG NLHFIRFPTQ DLPTFIQMGR DKNFSTLHTV LCATGGGAYK
     FEKDFRTIGN LHLHKLDELD CLVKGLLYID SVSFNGQAEC YYFANASEPE RCQKMPFNLD
     DPYPLLVVNI GSGVSILAVH SKDNYKRVTG TSLGGGTFLG LCSLLTGCES FEEALEMASK
     GDSTQADKLV RDIYGGDYER FGLPGWAVAS SFGNMIYKEK RESVSKEDLA RATLVTITNN
     IGSIARMCAV NEKINRVVFV GNFLRVNTLS MKLLAYALDY WSKGQLKALF LEHEGYFGAV
     GALLGLPNFS