PANC_FRATT
ID PANC_FRATT Reviewed; 261 AA.
AC Q5NF57;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=FTT_1390;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ749949; CAG46023.1; -; Genomic_DNA.
DR RefSeq; WP_003022190.1; NZ_CP010290.1.
DR RefSeq; YP_170335.1; NC_006570.2.
DR PDB; 3N8H; X-ray; 2.00 A; A/B=1-261.
DR PDB; 3QTT; X-ray; 2.60 A; A/B=1-258.
DR PDB; 5HG0; X-ray; 2.40 A; A/B=1-261.
DR PDBsum; 3N8H; -.
DR PDBsum; 3QTT; -.
DR PDBsum; 5HG0; -.
DR AlphaFoldDB; Q5NF57; -.
DR SMR; Q5NF57; -.
DR STRING; 177416.FTT_1390; -.
DR DNASU; 3191378; -.
DR EnsemblBacteria; CAG46023; CAG46023; FTT_1390.
DR KEGG; ftu:FTT_1390; -.
DR eggNOG; COG0414; Bacteria.
DR OMA; SRNKYLC; -.
DR UniPathway; UPA00028; UER00005.
DR EvolutionaryTrace; Q5NF57; -.
DR Proteomes; UP000001174; 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 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..261
FT /note="Pantothenate synthetase"
FT /id="PRO_0000305450"
FT ACT_SITE 36
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 60
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 60
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 147..150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 153
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 184..187
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:3N8H"
FT HELIX 7..15
FT /evidence="ECO:0007829|PDB:3N8H"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 34..46
FT /evidence="ECO:0007829|PDB:3N8H"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:3N8H"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:3N8H"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:3N8H"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:3N8H"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:3N8H"
FT HELIX 214..222
FT /evidence="ECO:0007829|PDB:3N8H"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:3N8H"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:3N8H"
FT STRAND 237..244
FT /evidence="ECO:0007829|PDB:3N8H"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:3N8H"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:3N8H"
SQ SEQUENCE 261 AA; 29715 MW; 9EF115B43EDC2FDE CRC64;
MIIADNIKQF HSIRNSLIKQ QKIGFVPTMG ALHNGHISLI KKAKSENDVV IVSIFVNPTQ
FNNPNDYQTY PNQLQQDIQI LASLDVDVLF NPSEKDIYPD GNLLRIEPKL EIANILEGKS
RPGHFSGMLT VVLKLLQITK PNNLYLGEKD YQQVMLIKQL VKDFFINTKI IVCPTQRQPS
GLPLSSRNKN LTSTDIEIAN KIYEILRQDD FSNLEELTNK INSTGAKLQY IQKLNNRIFL
AFYIGKVRLI DNFLKETGPS C
