COAX_PSEAE
ID COAX_PSEAE Reviewed; 248 AA.
AC Q9HWC1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Type III pantothenate kinase;
DE EC=2.7.1.33 {ECO:0000269|PubMed:16905099};
DE AltName: Full=PanK-III;
DE AltName: Full=Pantothenic acid kinase;
GN Name=coaX; Synonyms=coaA; OrderedLocusNames=PA4279;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APOPROTEIN AND COMPLEX WITH
RP SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, KINETIC
RP PARAMETERS, AND MUTAGENESIS OF ASN-9; LYS-13; ASP-101; ASP-121; HIS-156 AND
RP THR-157.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
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. Can utilize a wide range of phosphoryl
CC donors other than ATP, and does not discriminate between purine- and
CC pyrimidine-based nucleotides or deoxynucleotides. Is responsible for
CC the resistance of P.aeruginosa to the pantothenamide antibiotics, since
CC it cannot bind and phosphorylate these pantothenate analogs.
CC {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; Evidence={ECO:0000269|PubMed:16905099};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:16905099};
CC Name=NH4(+); Xref=ChEBI:CHEBI:28938;
CC Evidence={ECO:0000269|PubMed:16905099};
CC Note=Monovalent cations. Strong preference for ammonium over potassium.
CC {ECO:0000269|PubMed:16905099};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for pantothenate (in the absence of ammonium)
CC {ECO:0000269|PubMed:16905099};
CC KM=20 uM for pantothenate (in the presence of ammonium)
CC {ECO:0000269|PubMed:16905099};
CC KM=7.2 mM for ATP (in the absence of ammonium)
CC {ECO:0000269|PubMed:16905099};
CC KM=3.2 mM for ATP (in the presence of ammonium)
CC {ECO:0000269|PubMed:16905099};
CC Note=kcat is 12.5 min(-1) for the phosphorylation of pantothenate in
CC the absence of ammonium. kcat is 25 min(-1) for the phosphorylation
CC of pantothenate in the presence of ammonium.
CC {ECO:0000269|PubMed:16905099};
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:0000250}.
CC -!- SIMILARITY: Belongs to the type III pantothenate kinase family.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG07667.1; -; Genomic_DNA.
DR PIR; H83111; H83111.
DR RefSeq; NP_252969.1; NC_002516.2.
DR RefSeq; WP_003093768.1; NZ_QZGE01000028.1.
DR PDB; 2F9T; X-ray; 2.20 A; A/B=1-248.
DR PDB; 2F9W; X-ray; 1.90 A; A/B=1-248.
DR PDBsum; 2F9T; -.
DR PDBsum; 2F9W; -.
DR AlphaFoldDB; Q9HWC1; -.
DR SMR; Q9HWC1; -.
DR STRING; 287.DR97_3628; -.
DR ChEMBL; CHEMBL4295625; -.
DR PaxDb; Q9HWC1; -.
DR PRIDE; Q9HWC1; -.
DR DNASU; 881667; -.
DR EnsemblBacteria; AAG07667; AAG07667; PA4279.
DR GeneID; 881667; -.
DR KEGG; pae:PA4279; -.
DR PATRIC; fig|208964.12.peg.4480; -.
DR PseudoCAP; PA4279; -.
DR HOGENOM; CLU_066627_0_1_6; -.
DR InParanoid; Q9HWC1; -.
DR OMA; NSFIKWR; -.
DR PhylomeDB; Q9HWC1; -.
DR BioCyc; PAER208964:G1FZ6-4358-MON; -.
DR BRENDA; 2.7.1.33; 5087.
DR UniPathway; UPA00241; UER00352.
DR EvolutionaryTrace; Q9HWC1; -.
DR Proteomes; UP000002438; 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 GO; GO:0046677; P:response to antibiotic; 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 3D-structure; Antibiotic resistance; ATP-binding; Coenzyme A biosynthesis;
KW Cytoplasm; Kinase; Metal-binding; Nucleotide-binding; Potassium;
KW Reference proteome; Transferase.
FT CHAIN 1..248
FT /note="Type III pantothenate kinase"
FT /id="PRO_0000267575"
FT ACT_SITE 101
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 92
FT /ligand="substrate"
FT BINDING 99..102
FT /ligand="substrate"
FT BINDING 121
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000305|PubMed:16905099"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 180
FT /ligand="substrate"
FT MUTAGEN 9
FT /note="N->G: 96-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 13
FT /note="K->A: 7-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 101
FT /note="D->A: 5-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 121
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 156
FT /note="H->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:16905099"
FT MUTAGEN 157
FT /note="T->A: 2.5-fold reduction in activity."
FT /evidence="ECO:0000269|PubMed:16905099"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:2F9W"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 22..31
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:2F9W"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 58..71
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 100..113
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 117..131
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 180..207
FT /evidence="ECO:0007829|PDB:2F9W"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2F9W"
FT HELIX 236..244
FT /evidence="ECO:0007829|PDB:2F9W"
SQ SEQUENCE 248 AA; 26758 MW; 609D37480899DA3B CRC64;
MILELDCGNS LIKWRVIEGA ARSVAGGLAE SDDALVEQLT SQQALPVRAC RLVSVRSEQE
TSQLVARLEQ LFPVSALVAS SGKQLAGVRN GYLDYQRLGL DRWLALVAAH HLAKKACLVI
DLGTAVTSDL VAADGVHLGG YICPGMTLMR SQLRTHTRRI RYDDAEARRA LASLQPGQAT
AEAVERGCLL MLRGFVREQY AMACELLGPD CEIFLTGGDA ELVRDELAGA RIMPDLVFVG
LALACPIE
