PANC_THET8
ID PANC_THET8 Reviewed; 276 AA.
AC Q5SHF5; P83701;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=TTHA1775;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND SUBUNIT.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of pantothenate synthetase from Thermus thermophilus
RT HB8.";
RL Submitted (JUN-2003) to the PDB data bank.
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:0000305|Ref.2}.
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 -!- MISCELLANEOUS: PDB 1UFV apparently has a Val-49-Ala mutation.
CC -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00158}.
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DR EMBL; AP008226; BAD71598.1; -; Genomic_DNA.
DR RefSeq; WP_011173797.1; NC_006461.1.
DR RefSeq; YP_145041.1; NC_006461.1.
DR PDB; 1UFV; X-ray; 2.05 A; A/B=1-276.
DR PDB; 1V8F; X-ray; 1.90 A; A/B=1-276.
DR PDBsum; 1UFV; -.
DR PDBsum; 1V8F; -.
DR AlphaFoldDB; Q5SHF5; -.
DR SMR; Q5SHF5; -.
DR STRING; 300852.55773157; -.
DR DrugBank; DB03570; Tris-Hydroxymethyl-Methyl-Ammonium.
DR EnsemblBacteria; BAD71598; BAD71598; BAD71598.
DR GeneID; 3169469; -.
DR KEGG; ttj:TTHA1775; -.
DR PATRIC; fig|300852.9.peg.1745; -.
DR eggNOG; COG0414; Bacteria.
DR HOGENOM; CLU_047148_0_0_0; -.
DR OMA; CNHKLEP; -.
DR PhylomeDB; Q5SHF5; -.
DR UniPathway; UPA00028; UER00005.
DR EvolutionaryTrace; Q5SHF5; -.
DR Proteomes; UP000000532; 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; 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..276
FT /note="Pantothenate synthetase"
FT /id="PRO_0000128283"
FT ACT_SITE 32
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 25..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 56
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 56
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 143..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 149
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT BINDING 180..183
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:1V8F"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:1V8F"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:1V8F"
FT STRAND 44..50
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1V8F"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:1V8F"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1V8F"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:1V8F"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:1V8F"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 189..194
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 197..210
FT /evidence="ECO:0007829|PDB:1V8F"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:1V8F"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:1V8F"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:1V8F"
FT STRAND 256..263
FT /evidence="ECO:0007829|PDB:1V8F"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:1V8F"
SQ SEQUENCE 276 AA; 30695 MW; 975B6B82D162AE40 CRC64;
MRTVSTVAEL RAALPREGVG FVPTMGYLHR GHLALVERAR RENPFVVVSV FVNPLQFGPG
EDYHRYPRDL ERDRALLQEA GVDLLFAPGV EEMYPEGFAT RVQVEGPLTA LWEGAVRPGH
FQGVATVVAR LFLLVQPQRA YFGEKDYQQL LVVRRMVRDL GFPVEVVGVP TVREEDGLAL
SSRNVYLSPE TRKKAPVLYR ALLAMREVAG QGGSVAEALR AGEEALRAVP EFRKDYLAIV
HPETLLPLSD WVAGARGIVA GRFPEARLID NLEVYP
