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 03-AUG-2022, entry version 130.
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};
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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 AlphaFoldDB; P37564; -.
DR SMR; P37564; -.
DR STRING; 224308.BSU00700; -.
DR jPOST; P37564; -.
DR PaxDb; P37564; -.
DR PRIDE; P37564; -.
DR EnsemblBacteria; CAB11846; CAB11846; BSU_00700.
DR GeneID; 936960; -.
DR KEGG; bsu:BSU00700; -.
DR PATRIC; fig|224308.179.peg.70; -.
DR eggNOG; COG1521; Bacteria.
DR InParanoid; P37564; -.
DR OMA; HEPWLTL; -.
DR PhylomeDB; P37564; -.
DR BioCyc; BSUB:BSU00700-MON; -.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_01274; Pantothen_kinase_3; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004619; Type_III_PanK.
DR PANTHER; PTHR34265; PTHR34265; 1.
DR Pfam; PF03309; Pan_kinase; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR00671; baf; 1.
PE 1: Evidence at protein level;
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 ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107..110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255"
FT BINDING 132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 184
FT /ligand="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
