ID   PANC_BURTA              Reviewed;         279 AA.
AC   Q2T095;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 99.
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};
GN   OrderedLocusNames=BTH_I0848;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 /
OS   CIP 106301 / E264).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(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}.
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DR   EMBL; CP000086; ABC39343.1; -; Genomic_DNA.
DR   RefSeq; WP_009892491.1; NZ_CP008785.1.
DR   PDB; 3UK2; X-ray; 2.25 A; A/B=1-279.
DR   PDBsum; 3UK2; -.
DR   AlphaFoldDB; Q2T095; -.
DR   SMR; Q2T095; -.
DR   KEGG; bte:BTH_I0848; -.
DR   HOGENOM; CLU_047148_0_0_4; -.
DR   UniPathway; UPA00028; UER00005.
DR   Proteomes; UP000001930; Chromosome I.
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; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.30.1300.10; Pantoate-beta-alanine ligase, C-terminal domain; 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   NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR   NCBIfam; TIGR00018; panC; 1.
DR   PANTHER; PTHR21299; CYTIDYLATE KINASE/PANTOATE-BETA-ALANINE LIGASE; 1.
DR   PANTHER; PTHR21299:SF1; PANTOATE--BETA-ALANINE LIGASE; 1.
DR   Pfam; PF02569; Pantoate_ligase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Pantothenate biosynthesis.
FT   CHAIN           1..279
FT                   /note="Pantothenate synthetase"
FT                   /id="PRO_0000305418"
FT   ACT_SITE        33
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         57
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         57
FT                   /ligand="beta-alanine"
FT                   /ligand_id="ChEBI:CHEBI:57966"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         144..147
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         150
FT                   /ligand="(R)-pantoate"
FT                   /ligand_id="ChEBI:CHEBI:15980"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
FT   BINDING         181..184
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:3UK2"
FT   HELIX           7..13
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   STRAND          21..25
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           31..41
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   STRAND          45..51
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           55..57
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           71..79
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   TURN            80..82
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           91..94
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           107..110
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           114..117
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           121..136
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   STRAND          139..144
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           148..160
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   STRAND          166..170
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           183..187
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           190..195
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           198..211
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           217..230
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   STRAND          234..242
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   TURN            243..245
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   HELIX           251..255
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   STRAND          260..268
FT                   /evidence="ECO:0007829|PDB:3UK2"
FT   STRAND          271..279
FT                   /evidence="ECO:0007829|PDB:3UK2"
SQ   SEQUENCE   279 AA;  31400 MW;  49E306BA90AF6365 CRC64;
     MKVISSIQEL RDQLRGQNRT AFVPTMGNLH EGHLSLMRLA RQHGDPVVAS IFVNRLQFGP
     NEDFDKYPRT LQEDIEKLQK ENVYVLFAPT ERDMYPEPQE YRVQPPHDLG DILEGEFRPG
     FFTGVCTVVT KLMACVQPRV AVFGKKDYQQ LMIVRRMCQQ LALPVEIVAA ETVRDADGLA
     LSSRNRYLSE AERAEAPELA KTLARVRDAV LDGERDLAAI ERRAVAHLSA RGWQPDYVSI
     RRRENLVAPS AAQIEAGDPL VVLTAAKLGA TRLIDNLEI
//