(data stored in SCRATCH zone)

SWISSPROT: COAX_BACSU

ID   COAX_BACSU              Reviewed;         258 AA.
AC   P37564; Q5EC36;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   11-DEC-2019, entry version 122.
DE   RecName: Full=Type III pantothenate kinase;
DE            EC=2.7.1.33;
DE   AltName: Full=PanK-III;
DE   AltName: Full=Pantothenic acid kinase;
GN   Name=coaX; Synonyms=coaA, yacB; OrderedLocusNames=BSU00700;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CHARACTERIZATION, ACTIVITY
RP   REGULATION, AND KINETIC PARAMETERS.
RC   STRAIN=168;
RX   PubMed=15795230; DOI=10.1074/jbc.c500044200;
RA   Brand L.A., Strauss E.;
RT   "Characterization of a new pantothenate kinase isoform from Helicobacter
RT   pylori.";
RL   J. Biol. Chem. 280:20185-20188(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO C-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   FUNCTION, AND COFACTOR.
RC   STRAIN=168;
RX   PubMed=16905099; DOI=10.1016/j.str.2006.06.008;
RA   Hong B.S., Yun M.K., Zhang Y.-M., Chohnan S., Rock C.O., White S.W.,
RA   Jackowski S., Park H.-W., Leonardi R.;
RT   "Prokaryotic type II and type III pantothenate kinases: the same monomer
RT   fold creates dimers with distinct catalytic properties.";
RL   Structure 14:1251-1261(2006).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC       first step in CoA biosynthesis. Cannot utilize a phosphoryl donor other
CC       than ATP. {ECO:0000269|PubMed:15795230, ECO:0000269|PubMed:16905099}.
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;
CC   -!- COFACTOR:
CC       Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC         Evidence={ECO:0000269|PubMed:16905099};
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000269|PubMed:16905099};
CC       Note=Monovalent cations. Ammonium or potassium.
CC       {ECO:0000269|PubMed:16905099};
CC   -!- ACTIVITY REGULATION: Not regulated by feedback inhibition by CoA and
CC       its thioesters as described for many other pantothenate kinases. Not
CC       inhibited by N-pentylpantothenamide (N5-Pan), and this compound cannot
CC       act as a substrate either. {ECO:0000269|PubMed:15795230}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=168 uM for pantothenate {ECO:0000269|PubMed:15795230};
CC         KM=3.0 mM for ATP {ECO:0000269|PubMed:15795230};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC       pantothenate: step 1/5.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA05305.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; AY912104; AAW83041.2; -; Genomic_DNA.
DR   EMBL; D26185; BAA05305.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB11846.2; -; Genomic_DNA.
DR   PIR; S66100; S66100.
DR   RefSeq; NP_387951.2; NC_000964.3.
DR   RefSeq; WP_010886388.1; NZ_JNCM01000028.1.
DR   SMR; P37564; -.
DR   STRING; 224308.BSU00700; -.
DR   PaxDb; P37564; -.
DR   PRIDE; P37564; -.
DR   EnsemblBacteria; CAB11846; CAB11846; BSU00700.
DR   GeneID; 936960; -.
DR   KEGG; bsu:BSU00700; -.
DR   PATRIC; fig|224308.179.peg.70; -.
DR   eggNOG; COG1521; LUCA.
DR   HOGENOM; HOG000066025; -.
DR   InParanoid; P37564; -.
DR   KO; K03525; -.
DR   OMA; HEPWLTL; -.
DR   PhylomeDB; P37564; -.
DR   BioCyc; BSUB:BSU00700-MONOMER; -.
DR   SABIO-RK; P37564; -.
DR   UniPathway; UPA00241; UER00352.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004594; F:pantothenate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR   InterPro; IPR004619; Type_III_PanK.
DR   PANTHER; PTHR34265; PTHR34265; 1.
DR   Pfam; PF03309; Pan_kinase; 1.
DR   TIGRFAMs; TIGR00671; baf; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37564.
DR   SWISS-2DPAGE; P37564.
KW   ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase; Metal-binding;
KW   Nucleotide-binding; Potassium; Reference proteome; Transferase.
FT   CHAIN           1..258
FT                   /note="Type III pantothenate kinase"
FT                   /id="PRO_0000049448"
FT   NP_BIND         6..13
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
FT   REGION          107..110
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        109
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   METAL           129
FT                   /note="Monovalent cation"
FT                   /evidence="ECO:0000255"
FT   BINDING         100
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   BINDING         184
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        214..215
FT                   /note="EP -> KQ (in Ref. 1; AAW83041)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   258 AA;  28576 MW;  EB2BB7FECE46DEA2 CRC64;
     MLLVIDVGNT NTVLGVYHDG KLEYHWRIET SRHKTEDEFG MILRSLFDHS GLMFEQIDGI
     IISSVVPPIM FALERMCTKY FHIEPQIVGP GMKTGLNIKY DNPKEVGADR IVNAVAAIHL
     YGNPLIVVDF GTATTYCYID ENKQYMGGAI APGITISTEA LYSRAAKLPR IEITRPDNII
     GKNTVSAMQS GILFGYVGQV EGIVKRMKWQ AKQEPKVIAT GGLAPLIANE SDCIDIVDPF
     LTLKGLELIY ERNRVGSV
//

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