COAW_BACAN
ID COAW_BACAN Reviewed; 276 AA.
AC Q81PB2; Q6HXH8; Q6KRK2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Type II pantothenate kinase {ECO:0000255|HAMAP-Rule:MF_01273};
DE EC=2.7.1.33 {ECO:0000255|HAMAP-Rule:MF_01273};
DE AltName: Full=PanK-II {ECO:0000255|HAMAP-Rule:MF_01273};
DE AltName: Full=Pantothenic acid kinase {ECO:0000255|HAMAP-Rule:MF_01273};
GN Name=coaW {ECO:0000255|HAMAP-Rule:MF_01273};
GN OrderedLocusNames=BA_2901, GBAA_2901, BAS2702;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
CC -!- FUNCTION: Catalyzes the phosphorylation of pantothenate (Pan), the
CC first step in CoA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01273}.
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:0000255|HAMAP-Rule:MF_01273};
CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5. {ECO:0000255|HAMAP-Rule:MF_01273}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01273}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01273}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01273}.
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DR EMBL; AE016879; AAP26726.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT55011.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT32018.1; -; Genomic_DNA.
DR RefSeq; NP_845240.1; NC_003997.3.
DR RefSeq; WP_000446264.1; NZ_WXXJ01000007.1.
DR RefSeq; YP_028960.1; NC_005945.1.
DR AlphaFoldDB; Q81PB2; -.
DR SMR; Q81PB2; -.
DR STRING; 260799.BAS2702; -.
DR DNASU; 1088439; -.
DR EnsemblBacteria; AAP26726; AAP26726; BA_2901.
DR EnsemblBacteria; AAT32018; AAT32018; GBAA_2901.
DR GeneID; 45022724; -.
DR KEGG; ban:BA_2901; -.
DR KEGG; bar:GBAA_2901; -.
DR KEGG; bat:BAS2702; -.
DR PATRIC; fig|198094.11.peg.2881; -.
DR eggNOG; COG5146; Bacteria.
DR HOGENOM; CLU_087521_1_0_9; -.
DR OMA; VKHIYKD; -.
DR UniPathway; UPA00241; UER00352.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
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 HAMAP; MF_01273; Pantothen_kinase_2; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR004567; Type_II_PanK.
DR InterPro; IPR011602; Type_II_PanK_bac.
DR PANTHER; PTHR12280; PTHR12280; 1.
DR Pfam; PF03630; Fumble; 1.
DR PIRSF; PIRSF036940; PanK_bac_aCoA; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR00555; panK_eukar; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..276
FT /note="Type II pantothenate kinase"
FT /id="PRO_0000261337"
FT ACT_SITE 76
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 127..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01273"
SQ SEQUENCE 276 AA; 30060 MW; D8D423AA2A36AF9B CRC64;
MESTIGIDAG GTLTKIAYLN KKMQLAFEKV YSNEQNKIID WLKNQTGIKQ ICITGGKAKQ
LQQLLSASYK IVELNEFEAT LVGVRYILKK EKYDINNFVL TNIGTGTSIH YIYNDQYIRA
GGTGVGGGTI MGLSKLLTNI DHFEDVIPLT KVGSRKELDI TVGDIYGGIL SPIDNSLTAS
NFGKAAITDS NYNSSDILAT IQGLVGEVVT ALSLQFAETK NIDHIIYIGS TLCNNIHLQN
IISSYTKYQN KTPIFLRDGG NSGAIGALLY ATNKKS
