PANC_ARATH
ID PANC_ARATH Reviewed; 310 AA.
AC Q9FKB3; Q682X9;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Pantoate--beta-alanine ligase;
DE EC=6.3.2.1;
DE AltName: Full=Pantoate-activating enzyme;
DE AltName: Full=Pantothenate synthetase;
GN OrderedLocusNames=At5g48840; ORFNames=K24G6.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=16042590; DOI=10.1042/bst0330743;
RA Coxon K.M., Chakauya E., Ottenhof H.H., Whitney H.M., Blundell T.L.,
RA Abell C., Smith A.G.;
RT "Pantothenate biosynthesis in higher plants.";
RL Biochem. Soc. Trans. 33:743-746(2005).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, ALLOSTERIC PROPERTIES,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF GLU-132.
RX PubMed=17040917; DOI=10.1074/jbc.m607895200;
RA Jonczyk R., Genschel U.;
RT "Molecular adaptation and allostery in plant pantothenate synthetases.";
RL J. Biol. Chem. 281:37435-37446(2006).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17932772; DOI=10.1007/s11103-007-9248-6;
RA Jonczyk R., Ronconi S., Rychlik M., Genschel U.;
RT "Pantothenate synthetase is essential but not limiting for pantothenate
RT biosynthesis in Arabidopsis.";
RL Plant Mol. Biol. 66:1-14(2008).
CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine to
CC form pantothenate. Essential for panthotenate biosynthesis.
CC {ECO:0000269|PubMed:17040917, ECO:0000269|PubMed:17932772}.
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:0000269|PubMed:17040917};
CC -!- ACTIVITY REGULATION: Enzyme kinetics do not match Michaelis-Menten
CC kinetics, suggesting allosteric behavior. Inhibited by high pantoate
CC levels. {ECO:0000269|PubMed:17040917}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:17040917};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantothenate from (R)-pantoate and beta-alanine: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17040917}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16042590}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves, stems,
CC cauline leaves, stigma, sepals and petals.
CC {ECO:0000269|PubMed:17932772}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality due to arrest of
CC embryogenesis at the preglobular stage when homozygous.
CC {ECO:0000269|PubMed:17932772}.
CC -!- SIMILARITY: Belongs to the pantothenate synthetase family.
CC {ECO:0000305}.
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DR EMBL; AB012242; BAB09437.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95732.1; -; Genomic_DNA.
DR EMBL; AK175238; BAD43001.1; -; mRNA.
DR RefSeq; NP_199695.1; NM_124261.4.
DR AlphaFoldDB; Q9FKB3; -.
DR SMR; Q9FKB3; -.
DR STRING; 3702.AT5G48840.1; -.
DR PaxDb; Q9FKB3; -.
DR PRIDE; Q9FKB3; -.
DR ProteomicsDB; 248656; -.
DR EnsemblPlants; AT5G48840.1; AT5G48840.1; AT5G48840.
DR GeneID; 834942; -.
DR Gramene; AT5G48840.1; AT5G48840.1; AT5G48840.
DR KEGG; ath:AT5G48840; -.
DR Araport; AT5G48840; -.
DR TAIR; locus:2156564; AT5G48840.
DR eggNOG; KOG3042; Eukaryota.
DR HOGENOM; CLU_047148_2_0_1; -.
DR InParanoid; Q9FKB3; -.
DR OMA; CNHKLEP; -.
DR OrthoDB; 1399179at2759; -.
DR PhylomeDB; Q9FKB3; -.
DR BioCyc; ARA:AT5G48840-MON; -.
DR BioCyc; MetaCyc:AT5G48840-MON; -.
DR BRENDA; 6.3.2.1; 399.
DR UniPathway; UPA00028; UER00005.
DR PRO; PR:Q9FKB3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKB3; baseline and differential.
DR Genevisible; Q9FKB3; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004592; F:pantoate-beta-alanine ligase activity; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:TAIR.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IMP:TAIR.
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 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW Pantothenate biosynthesis; Reference proteome.
FT CHAIN 1..310
FT /note="Pantoate--beta-alanine ligase"
FT /id="PRO_0000128299"
FT ACT_SITE 39
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="beta-alanine"
FT /ligand_id="ChEBI:CHEBI:57966"
FT /evidence="ECO:0000250"
FT BINDING 175..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="(R)-pantoate"
FT /ligand_id="ChEBI:CHEBI:15980"
FT /evidence="ECO:0000250"
FT BINDING 212..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 132
FT /note="E->A: Reduces allosteric properties."
FT /evidence="ECO:0000269|PubMed:17040917"
SQ SEQUENCE 310 AA; 34137 MW; AD07D927625AD1A6 CRC64;
MEPEVIRDKD SMRKWSRAMR SQGKTIGLVP TMGYLHEGHL SLVRQSLALT DVTVVSIYVN
PGQFSPTEDL STYPSDFSGD LTKLAALSGG KVVVFNPKNL YDYGGETKKI NDGGGNGGRV
VSCVEEGGLG HETWIRVERL EKGFCGKSRP VFFRGVATIV TKLFNIVEPD VALFGKKDYQ
QWRIIQRMVR DLNFGIEIVG SDIAREKDGL AMSSRNVRLS DEERQRALSI SRSLAMAKAS
VAEGKTNCAE LKDMIIQQVV GSAGRVDYVE IVDQETLEGV EEIKSGVVIC VAAWFGTVRL
IDNIEINVSL
