PANC_BURCH
ID PANC_BURCH Reviewed; 279 AA.
AC A0K9L5;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Bcen2424_2442;
OS Burkholderia cenocepacia (strain HI2424).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=331272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI2424;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F.,
RA Konstantinidis K., Tiedje J.M., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000458; ABK09192.1; -; Genomic_DNA.
DR RefSeq; WP_011545961.1; NC_008542.1.
DR AlphaFoldDB; A0K9L5; -.
DR SMR; A0K9L5; -.
DR KEGG; bch:Bcen2424_2442; -.
DR HOGENOM; CLU_047148_0_0_4; -.
DR OMA; CNHKLEP; -.
DR OrthoDB; 1661843at2; -.
DR UniPathway; UPA00028; UER00005.
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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis.
FT CHAIN 1..279
FT /note="Pantothenate synthetase"
FT /id="PRO_0000305413"
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"
SQ SEQUENCE 279 AA; 31452 MW; 35A524A632CB1E63 CRC64;
MKVISSIQEL RDQLRGQNRT AFVPTMGNLH EGHLSLMRLA RQHGDPVVAS IFVNRLQFGP
NEDFDKYPRT LQDDIEKLQQ NNVYVLFAPT ERDMYPEPQE YRVLPPDDLG GILEGEFRPG
FFAGVCTVVT KLMSCVQPRV AVFGKKDYQQ LMIVRRMCQQ LALPVEIIAA ETVRDEDGLA
LSSRNRYLTT DERKEAPELA KTLQRVRDSV LGGERDLGKL EQHAHTHLAE RGWVPDYIAI
RRRANLIAPS AAELEAGEPL VVLAAAKLGA TRLIDNLEI