ID   PANK_SCHPO              Reviewed;         403 AA.
AC   O74962;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Pantothenate kinase;
DE            EC=2.7.1.33;
DE   AltName: Full=Pantothenic acid kinase;
GN   ORFNames=SPBC4B4.01c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1] {ECO:0000312|EMBL:CAA19281.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2] {ECO:0000305}
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-82 AND SER-84, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Plays a role in the physiological regulation of the
CC       intracellular CoA concentration. {ECO:0000250|UniProtKB:Q8K4K6}.
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:Q8K4K6};
CC   -!- ACTIVITY REGULATION: Regulated by feedback inhibition by malonyl-CoA.
CC       {ECO:0000250|UniProtKB:Q04430}.
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC       {ECO:0000255}.
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DR   EMBL; CU329671; CAA19281.1; -; Genomic_DNA.
DR   PIR; T40473; T40473.
DR   RefSeq; NP_596418.1; NM_001022337.2.
DR   AlphaFoldDB; O74962; -.
DR   SMR; O74962; -.
DR   STRING; 4896.SPBC4B4.01c.1; -.
DR   iPTMnet; O74962; -.
DR   MaxQB; O74962; -.
DR   PaxDb; O74962; -.
DR   PRIDE; O74962; -.
DR   EnsemblFungi; SPBC4B4.01c.1; SPBC4B4.01c.1:pep; SPBC4B4.01c.
DR   GeneID; 2540815; -.
DR   KEGG; spo:SPBC4B4.01c; -.
DR   PomBase; SPBC4B4.01c; -.
DR   VEuPathDB; FungiDB:SPBC4B4.01c; -.
DR   eggNOG; KOG2201; Eukaryota.
DR   HOGENOM; CLU_011154_3_0_1; -.
DR   InParanoid; O74962; -.
DR   OMA; WAQEGDN; -.
DR   PhylomeDB; O74962; -.
DR   UniPathway; UPA00241; UER00352.
DR   PRO; PR:O74962; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004594; F:pantothenate kinase activity; ISS:PomBase.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; ISS:PomBase.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Transferase.
FT   CHAIN           1..403
FT                   /note="Pantothenate kinase"
FT                   /id="PRO_0000316854"
FT   MOD_RES         80
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   403 AA;  44861 MW;  E4574392867BFE20 CRC64;
     MSETECGRFS TISRETISNV ERQLSQPPSV WLNLTGARII ENEGQFDKDI ALPNNKSHVT
     HIAVDIGGSL AKVMYYVCES SSPSSSSSSI SEAENYTGGR LSFMIFETAK IEDCIQFMAN
     LIDNHVKNCN KKKITLIATG GGAYKFYDRM SKQLDIKVIR EDEMECLIMG LNYFVSCIPR
     EVFVLDLDTC ELTFQNHLNC YHYPHMLVNI GSGVSILKVT GPSQFERIGG SSLGGGTLWG
     LLSLLTPANS FDEMLELSKG GDNTSVDMLV GDIYGKDIGY ERFGLKSTTI ASSFGKVFRE
     RKPLEEFAPQ DISRSLLLAI SNNIGQIAYL HAQKHNVQNI YFGGSFIRNH VQTMHTLTYA
     IQYWSNHTMN AYFLRHEGYL GVFGAFMKYA TSQPSNVPVP SIS