PANC_STAAR
ID PANC_STAAR Reviewed; 283 AA.
AC Q6GDK5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Pantothenate synthetase {ECO:0000255|HAMAP-Rule:MF_00158};
DE Short=PS {ECO:0000255|HAMAP-Rule:MF_00158};
DE EC=6.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00158};
DE AltName: Full=Pantoate--beta-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00158};
DE AltName: Full=Pantoate-activating enzyme {ECO:0000255|HAMAP-Rule:MF_00158};
GN Name=panC {ECO:0000255|HAMAP-Rule:MF_00158}; OrderedLocusNames=SAR2676;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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).
CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP +
CC diphosphate + H(+); Xref=Rhea:RHEA:10912, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:29032, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57966, ChEBI:CHEBI:456215; EC=6.3.2.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00158};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC mechanism. {ECO:0000255|HAMAP-Rule:MF_00158}.
CC -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00158}.
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DR EMBL; BX571856; CAG41653.1; -; Genomic_DNA.
DR RefSeq; WP_000163741.1; NC_002952.2.
DR PDB; 2X3F; X-ray; 1.95 A; A/B=1-283.
DR PDBsum; 2X3F; -.
DR AlphaFoldDB; Q6GDK5; -.
DR SMR; Q6GDK5; -.
DR KEGG; sar:SAR2676; -.
DR HOGENOM; CLU_047148_0_0_9; -.
DR OMA; CNHKLEP; -.
DR OrthoDB; 1661843at2; -.
DR UniPathway; UPA00028; UER00005.
DR EvolutionaryTrace; Q6GDK5; -.
DR Proteomes; UP000000596; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00560; PanC; 1.
DR Gene3D; 3.30.1300.10; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00158; PanC; 1.
DR InterPro; IPR003721; Pantoate_ligase.
DR InterPro; IPR042176; Pantoate_ligase_C.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21299:SF1; PTHR21299:SF1; 1.
DR Pfam; PF02569; Pantoate_ligase; 1.
DR TIGRFAMs; TIGR00018; panC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis.
FT CHAIN 1..283
FT /note="Pantothenate synthetase"
FT /id="PRO_0000128270"
FT ACT_SITE 38
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 62
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 62
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 148..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 154
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 185..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 8..21
FT /evidence="ECO:0007829|PDB:2X3F"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:2X3F"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:2X3F"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:2X3F"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:2X3F"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 125..140
FT /evidence="ECO:0007829|PDB:2X3F"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 152..165
FT /evidence="ECO:0007829|PDB:2X3F"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 194..200
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:2X3F"
FT HELIX 221..233
FT /evidence="ECO:0007829|PDB:2X3F"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:2X3F"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:2X3F"
FT STRAND 259..268
FT /evidence="ECO:0007829|PDB:2X3F"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:2X3F"
SQ SEQUENCE 283 AA; 31419 MW; C8A58E6F0F2679E7 CRC64;
MTKLITTVKE MQHIVKAAKR SGTTIGFIPT MGALHDGHLT MVRESVSTND ITVVSVFVNP
LQFGPNEDFD AYPRQIDKDL ELVSEVGADI VFHPAVEDMY PGELGIDVKV GPLADVLEGA
KRPGHFDGVV TVVNKLFNIV MPDYAYFGKK DAQQLAIVEQ MVKDFNHAVE IIGIDIVREA
DGLAKSSRNV YLTEQERQEA VHLSKSLLLA QALYQDGERQ SKVIIDKVTQ YLESHISGRI
EEVAVYSYPQ LVEQHEITGR IFISLAVKFS KARLIDNIII GAE
