PANC_ECOLI
ID PANC_ECOLI Reviewed; 283 AA.
AC P31663; Q2MCG4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Pantothenate synthetase;
DE Short=PS;
DE EC=6.3.2.1;
DE AltName: Full=Pantoate--beta-alanine ligase;
DE AltName: Full=Pantoate-activating enzyme;
GN Name=panC; OrderedLocusNames=b0133, JW0129;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8837478; DOI=10.1111/j.1574-6968.1996.tb08488.x;
RA Merkel W.K., Nichols B.P.;
RT "Characterization and sequence of the Escherichia coli panBCD gene
RT cluster.";
RL FEMS Microbiol. Lett. 143:247-252(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, AND ACTIVITY
RP REGULATION.
RC STRAIN=B;
RX PubMed=357689; DOI=10.3177/jnsv.24.243;
RA Miyatake K., Nakano Y., Kitaoka S.;
RT "Enzymological properties of pantothenate synthetase from Escherichia coli
RT B.";
RL J. Nutr. Sci. Vitaminol. 24:243-253(1978).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=11377204; DOI=10.1016/s0969-2126(01)00604-9;
RA von Delft F., Lewendon A., Dhanaraj V., Blundell T.L., Abell C.,
RA Smith A.G.;
RT "The crystal structure of E. coli pantothenate synthetase confirms it as a
RT member of the cytidylyltransferase superfamily.";
RL Structure 9:439-450(2001).
CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in
CC an ATP-dependent reaction via a pantoyl-adenylate intermediate.
CC {ECO:0000269|PubMed:357689}.
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 -!- ACTIVITY REGULATION: Activation requires a combination of a divalent
CC cation, magnesium or manganese, and a monovalent cation, potassium or
CC ammonium. Above the optimum concentration for activation, magnesium and
CC manganese are rather inhibitory. Also activated by 2-mercaptoethanol,
CC dithiothreitol, cysteine and glutathione. Inhibited by divalent cations
CC (mercury, cobalt, zinc, copper, silver), chelating agents (EDTA, EGTA
CC and o-phenanthroline), and analogs of beta-alanine (taurine, gamma-
CC aminobutyrate, gamma-amino-beta-hydroxybutyrate).
CC {ECO:0000269|PubMed:357689}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for pantoate {ECO:0000269|PubMed:357689};
CC KM=100 uM for ATP {ECO:0000269|PubMed:357689};
CC KM=150 uM for beta-alanine {ECO:0000269|PubMed:357689};
CC KM=2000 uM for magnesium {ECO:0000269|PubMed:357689};
CC KM=5500 uM for manganese {ECO:0000269|PubMed:357689};
CC pH dependence:
CC Optimum pH is 10. Stable from pH 5.0 to 11.0.
CC {ECO:0000269|PubMed:357689};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius. Stable up to 37 degrees
CC Celsius and loses activity almost completely when incubated at 60
CC degrees Celsius for 10 minutes. {ECO:0000269|PubMed:357689};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11377204}.
CC -!- INTERACTION:
CC P31663; P31663: panC; NbExp=5; IntAct=EBI-545354, EBI-545354;
CC P31663; P65556: yfcD; NbExp=6; IntAct=EBI-545354, EBI-545346;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=31601.2; Mass_error=3.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11377204};
CC -!- MISCELLANEOUS: The reaction proceeds by a bi uni uni bi ping pong
CC mechanism.
CC -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC {ECO:0000305}.
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DR EMBL; L17086; AAA24272.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73244.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76042.1; -; Genomic_DNA.
DR PIR; E64736; E64736.
DR RefSeq; NP_414675.1; NC_000913.3.
DR RefSeq; WP_000905383.1; NZ_LN832404.1.
DR PDB; 1IHO; X-ray; 1.70 A; A/B=1-283.
DR PDB; 3GUZ; X-ray; 1.67 A; A/B=1-176.
DR PDBsum; 1IHO; -.
DR PDBsum; 3GUZ; -.
DR AlphaFoldDB; P31663; -.
DR SMR; P31663; -.
DR BioGRID; 4261166; 157.
DR BioGRID; 849355; 1.
DR DIP; DIP-10437N; -.
DR IntAct; P31663; 11.
DR MINT; P31663; -.
DR STRING; 511145.b0133; -.
DR SWISS-2DPAGE; P31663; -.
DR jPOST; P31663; -.
DR PaxDb; P31663; -.
DR PRIDE; P31663; -.
DR EnsemblBacteria; AAC73244; AAC73244; b0133.
DR EnsemblBacteria; BAE76042; BAE76042; BAE76042.
DR GeneID; 66671578; -.
DR GeneID; 944958; -.
DR KEGG; ecj:JW0129; -.
DR KEGG; eco:b0133; -.
DR PATRIC; fig|1411691.4.peg.2148; -.
DR EchoBASE; EB1696; -.
DR eggNOG; COG0414; Bacteria.
DR HOGENOM; CLU_047148_0_0_6; -.
DR InParanoid; P31663; -.
DR OMA; CNHKLEP; -.
DR PhylomeDB; P31663; -.
DR BioCyc; EcoCyc:PANTOATE-BETA-ALANINE-LIG-MON; -.
DR BioCyc; MetaCyc:PANTOATE-BETA-ALANINE-LIG-MON; -.
DR BRENDA; 6.3.2.1; 2026.
DR SABIO-RK; P31663; -.
DR UniPathway; UPA00028; UER00005.
DR EvolutionaryTrace; P31663; -.
DR PRO; PR:P31663; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IDA:EcoCyc.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IMP:EcoCyc.
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..283
FT /note="Pantothenate synthetase"
FT /id="PRO_0000128229"
FT ACT_SITE 37
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000250"
FT BINDING 149..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 186..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:3GUZ"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:3GUZ"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:3GUZ"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:3GUZ"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1IHO"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:1IHO"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:3GUZ"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:3GUZ"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3GUZ"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:1IHO"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:1IHO"
FT HELIX 203..216
FT /evidence="ECO:0007829|PDB:1IHO"
FT HELIX 222..236
FT /evidence="ECO:0007829|PDB:1IHO"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:1IHO"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:1IHO"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:1IHO"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:1IHO"
SQ SEQUENCE 283 AA; 31598 MW; 4246647C6FDAFB20 CRC64;
MLIIETLPLL RQQIRRLRME GKRVALVPTM GNLHDGHMKL VDEAKARADV VVVSIFVNPM
QFDRPEDLAR YPRTLQEDCE KLNKRKVDLV FAPSVKEIYP NGTETHTYVD VPGLSTMLEG
ASRPGHFRGV STIVSKLFNL VQPDIACFGE KDFQQLALIR KMVADMGFDI EIVGVPIMRA
KDGLALSSRN GYLTAEQRKI APGLYKVLSS IADKLQAGER DLDEIITIAG QELNEKGFRA
DDIQIRDADT LLEVSETSKR AVILVAAWLG DARLIDNKMV ELA
