PANC_SALTY
ID PANC_SALTY Reviewed; 284 AA.
AC Q8ZRR1;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=STM0181;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL19145.1; -; Genomic_DNA.
DR RefSeq; NP_459186.1; NC_003197.2.
DR RefSeq; WP_000905344.1; NC_003197.2.
DR PDB; 3MUE; X-ray; 2.70 A; A/B/C/D=1-284.
DR PDBsum; 3MUE; -.
DR AlphaFoldDB; Q8ZRR1; -.
DR SMR; Q8ZRR1; -.
DR STRING; 99287.STM0181; -.
DR PaxDb; Q8ZRR1; -.
DR EnsemblBacteria; AAL19145; AAL19145; STM0181.
DR GeneID; 1251699; -.
DR KEGG; stm:STM0181; -.
DR PATRIC; fig|99287.12.peg.191; -.
DR HOGENOM; CLU_047148_0_0_6; -.
DR OMA; CNHKLEP; -.
DR PhylomeDB; Q8ZRR1; -.
DR BioCyc; SENT99287:STM0181-MON; -.
DR UniPathway; UPA00028; UER00005.
DR EvolutionaryTrace; Q8ZRR1; -.
DR Proteomes; UP000001014; 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; IPR004821; Cyt_trans-like.
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; TIGR00125; cyt_tran_rel; 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..284
FT /note="Pantothenate synthetase"
FT /id="PRO_0000128266"
FT ACT_SITE 37
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 61
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 61
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 149..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 155
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 186..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:3MUE"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:3MUE"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 65..69
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:3MUE"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:3MUE"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3MUE"
FT TURN 112..116
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:3MUE"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:3MUE"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:3MUE"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:3MUE"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:3MUE"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3MUE"
FT STRAND 259..269
FT /evidence="ECO:0007829|PDB:3MUE"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:3MUE"
SQ SEQUENCE 284 AA; 31858 MW; 219D5B538BE37E1D CRC64;
MLIIETLPLL RQHIRRLRQE GKRVALVPTM GNLHDGHMKL VDEAKARADV VIVSIFVNPM
QFDRPDDLVR YPRTLQEDCE KLNKRKVDYV FAPAVEEIYP HGLEGQTYVD VPGLSTMLEG
ASRPGHFRGV STIVSKLFNL IQPDIACFGE KDFQQLALIR KMVADMSYDI EIVGVPIIRA
KDGLALSSRN AYLTAEQRKI APGLYNVMNS IAEKLIAGNR ELQEIIAIAE QELNEKGFRA
DDIQIRDADT LLELTETSKR AVILAAAWLG QARLIDNQSV TLAQ
