PANC_THEMA
ID PANC_THEMA Reviewed; 280 AA.
AC Q9X0G6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 129.
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=TM_1077;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD36154.1; -; Genomic_DNA.
DR PIR; E72296; E72296.
DR RefSeq; NP_228883.1; NC_000853.1.
DR RefSeq; WP_004080408.1; NZ_CP011107.1.
DR PDB; 2EJC; X-ray; 2.40 A; A=1-280.
DR PDBsum; 2EJC; -.
DR AlphaFoldDB; Q9X0G6; -.
DR SMR; Q9X0G6; -.
DR STRING; 243274.THEMA_08970; -.
DR EnsemblBacteria; AAD36154; AAD36154; TM_1077.
DR KEGG; tma:TM1077; -.
DR eggNOG; COG0414; Bacteria.
DR InParanoid; Q9X0G6; -.
DR OMA; CNHKLEP; -.
DR OrthoDB; 1661843at2; -.
DR UniPathway; UPA00028; UER00005.
DR EvolutionaryTrace; Q9X0G6; -.
DR Proteomes; UP000008183; 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..280
FT /note="Pantothenate synthetase"
FT /id="PRO_0000128280"
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 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 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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:2EJC"
FT HELIX 7..19
FT /evidence="ECO:0007829|PDB:2EJC"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 35..47
FT /evidence="ECO:0007829|PDB:2EJC"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:2EJC"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2EJC"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2EJC"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 124..139
FT /evidence="ECO:0007829|PDB:2EJC"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 151..163
FT /evidence="ECO:0007829|PDB:2EJC"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 201..214
FT /evidence="ECO:0007829|PDB:2EJC"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:2EJC"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:2EJC"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:2EJC"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:2EJC"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:2EJC"
SQ SEQUENCE 280 AA; 32757 MW; 0BD1E4C572197163 CRC64;
MRIIETIEEM KKFSEEMREK KKTIGFVPTM GYLHEGHLSL VRRARAENDV VVVSIFVNPT
QFGPNEDYER YPRDFERDRK LLEKENVDCI FHPSVEEMYP PDFSTYVEET KLSKHLCGRS
RPGHFRGVCT VVTKLFNIVK PHRAYFGQKD AQQFRVLRRM VRDLNMDVEM IECPIVREPD
GLAMSSRNVY LSPEERQQAL SLYQSLKIAE NLYLNGERDA EKIKEEMIKH LSRFDKVKID
YVEIVDEETL EPVEKIDRKV IVAVAAWVGN ARLIDNTILG
