PANC_STAA8
ID PANC_STAA8 Reviewed; 283 AA.
AC Q2FV22;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
GN OrderedLocusNames=SAOUHSC_02918;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD31913.1; -; Genomic_DNA.
DR RefSeq; WP_000163734.1; NZ_LS483365.1.
DR RefSeq; YP_501370.1; NC_007795.1.
DR PDB; 3AG5; X-ray; 2.50 A; A/B=1-283.
DR PDB; 3AG6; X-ray; 1.85 A; A/B=1-283.
DR PDBsum; 3AG5; -.
DR PDBsum; 3AG6; -.
DR AlphaFoldDB; Q2FV22; -.
DR SMR; Q2FV22; -.
DR STRING; 1280.SAXN108_2867; -.
DR EnsemblBacteria; ABD31913; ABD31913; SAOUHSC_02918.
DR GeneID; 3921369; -.
DR KEGG; sao:SAOUHSC_02918; -.
DR PATRIC; fig|93061.5.peg.2637; -.
DR eggNOG; COG0414; Bacteria.
DR HOGENOM; CLU_047148_0_0_9; -.
DR OMA; CNHKLEP; -.
DR BRENDA; 6.3.2.1; 3352.
DR UniPathway; UPA00028; UER00005.
DR PRO; PR:Q2FV22; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IBA:GO_Central.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..283
FT /note="Pantothenate synthetase"
FT /id="PRO_0000305560"
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:3AG6"
FT HELIX 8..20
FT /evidence="ECO:0007829|PDB:3AG6"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:3AG6"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3AG6"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 76..86
FT /evidence="ECO:0007829|PDB:3AG6"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:3AG6"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 125..140
FT /evidence="ECO:0007829|PDB:3AG6"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:3AG6"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 187..191
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:3AG6"
FT HELIX 221..235
FT /evidence="ECO:0007829|PDB:3AG6"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:3AG6"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3AG6"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:3AG6"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:3AG6"
SQ SEQUENCE 283 AA; 31534 MW; 553C07138066CC97 CRC64;
MTKLITTVKE MQHIVKAAKR SGTTIGFIPT MGALHDGHLT MVRESVSTND ITIVSVFVNP
LQFGPNEDFD AYPRQIDKDL ELVSEVGADI VFHPAVEDMY PGELGIDVKV GPLADVLEGA
KRPGHFDGVV TVVNKLFNIV MPDYAYFGKK DAQQLAIVEQ MVKDFNHAVE IIGIDIVREA
DGLAKSSRNV YLTEQERQEA VHLSKSLLLA QALYQDGERQ SKVIIDRVTE YLESHISERI
EEVAVYSYPQ LVEQHEITGR IFISLAVKFS KARLIDNIII GAE
