PANC_BURTA
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 03-AUG-2022, entry version 91.
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=BTH_I0848;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; 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 / 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}.
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; 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 PRIDE; Q2T095; -.
DR EnsemblBacteria; ABC39343; ABC39343; BTH_I0848.
DR KEGG; bte:BTH_I0848; -.
DR HOGENOM; CLU_047148_0_0_4; -.
DR OMA; CNHKLEP; -.
DR OrthoDB; 1661843at2; -.
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; 3.30.1300.10; -; 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.
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
