PANC_HERAR
ID PANC_HERAR Reviewed; 279 AA.
AC A4G3S0;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, 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}; OrderedLocusNames=HEAR0974;
OS Herminiimonas arsenicoxydans.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herminiimonas.
OX NCBI_TaxID=204773;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ULPAs1;
RX PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA Lett M.-C., Danchin A., Bertin P.N.;
RT "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT environments.";
RL PLoS Genet. 3:518-530(2007).
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; CU207211; CAL61157.1; -; Genomic_DNA.
DR RefSeq; WP_011870495.1; NC_009138.1.
DR AlphaFoldDB; A4G3S0; -.
DR SMR; A4G3S0; -.
DR STRING; 204773.HEAR0974; -.
DR EnsemblBacteria; CAL61157; CAL61157; HEAR0974.
DR KEGG; har:HEAR0974; -.
DR eggNOG; COG0414; Bacteria.
DR HOGENOM; CLU_047148_0_0_4; -.
DR OMA; CNHKLEP; -.
DR OrthoDB; 1661843at2; -.
DR UniPathway; UPA00028; UER00005.
DR Proteomes; UP000006697; 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; 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; TIGR00018; panC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis; Reference proteome.
FT CHAIN 1..279
FT /note="Pantothenate synthetase"
FT /id="PRO_0000305466"
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 181..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00158"
SQ SEQUENCE 279 AA; 31383 MW; 00E5962088EF0A66 CRC64;
MKIISCIEEL RDHLRGQLRT AFVPTMGNLH DGHLSLMRLA RKHGDPVVAS IFVNRLQFGP
NEDFDRYPRT FQADVEKLEK EGVYILFAPT EKDLYPEPQE FRVQPPNDLG NTLEGEFRPG
FFSGVTTIVL KLFSCVQPSV AVFGKKDYQQ LMIVRNMSKQ FALPTEIIAA ETYRAEDGLA
LSSRNMYLSA EERAEAPALF KSLNAVANEV RSGHLDIFQL ERQAMADLSQ RGWKPDYISI
RKRSNLQPPS AGDMAQGEKL VVLAAAKLGA TRLIDNLEI
