COAW_STAAS
ID COAW_STAAS Reviewed; 267 AA.
AC Q6G7I0;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Type II pantothenate kinase;
DE EC=2.7.1.33;
DE AltName: Full=PanK-II;
DE AltName: Full=Pantothenic acid kinase;
GN Name=coaW; Synonyms=coaA; OrderedLocusNames=SAS2033;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH ATP ANALOG,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASP-6; THR-10; LEU-11; LYS-13;
RP GLU-70; TYR-137 AND LEU-263.
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. {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 -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-
CC pantothenate: step 1/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16905099}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type II pantothenate kinase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571857; CAG43841.1; -; Genomic_DNA.
DR RefSeq; WP_000862727.1; NC_002953.3.
DR PDB; 2EWS; X-ray; 2.05 A; A/B=1-267.
DR PDB; 4NB4; X-ray; 2.25 A; A/B/C/D/E/F/G/H=1-267.
DR PDBsum; 2EWS; -.
DR PDBsum; 4NB4; -.
DR AlphaFoldDB; Q6G7I0; -.
DR SMR; Q6G7I0; -.
DR ChEMBL; CHEMBL4295609; -.
DR KEGG; sas:SAS2033; -.
DR HOGENOM; CLU_087521_1_0_9; -.
DR OMA; VKHIYKD; -.
DR BRENDA; 2.7.1.33; 3352.
DR UniPathway; UPA00241; UER00352.
DR EvolutionaryTrace; Q6G7I0; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Coenzyme A biosynthesis; Cytoplasm; Kinase;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..267
FT /note="Type II pantothenate kinase"
FT /id="PRO_0000261346"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT BINDING 6..13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 121..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 137
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 6
FT /note="D->A: Abolishes enzymatic activity. Fails to bind
FT ATP."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 10
FT /note="T->A: Very low enzymatic activity. Still binds ATP."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 11
FT /note="L->A: Less active protein."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 13
FT /note="K->A: Abolishes enzymatic activity. Fails to bind
FT ATP."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 70
FT /note="E->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 137
FT /note="Y->A: Very low enzymatic activity."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 263
FT /note="L->P: Very low enzymatic activity."
FT /evidence="ECO:0000269|PubMed:16905099"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 22..28
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 32..40
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4NB4"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 92..106
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 137..144
FT /evidence="ECO:0007829|PDB:2EWS"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2EWS"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:2EWS"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 189..214
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:2EWS"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2EWS"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:2EWS"
SQ SEQUENCE 267 AA; 29097 MW; 3663BBC6DFBC2D9A CRC64;
MKVGIDAGGT LIKIVQEQDN QRTFKTELTK NIDQVVEWLN QQQIEKLCLT GGNAGVIAEN
INIPAQIFVE FDAASQGLGI LLKEQGHDLA DYIFANVGTG TSLHYFDGQS QRRVGGIGTG
GGMIQGLGYL LSQITDYKQL TDMAQHGDRN TIDLKVRHIY KDTEPPIPGD LTAANFGHVL
HHLDADFTPS NKLAAVIGVV GEVVTTMAIT VAREFKTENI VYIGSSFHNN ALLRKVVEDY
TVLRGCKPYY VENGAFSGAI GALYLEK
