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Q9FKB3 (PANC_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantoate--beta-alanine ligase

EC=6.3.2.1
Alternative name(s):
Pantoate-activating enzyme
Pantothenate synthetase
Gene names
Ordered Locus Names:At5g48840
ORF Names:K24G6.18
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the condensation of pantoate with beta-alanine to form pantothenate. Essential for panthotenate biosynthesis. Ref.5 Ref.6

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. Ref.5

Enzyme regulation

Enzyme kinetics do not match Michaelis-Menten kinetics, suggesting allosteric behavior. Inhibited by high pantoate levels. Ref.5

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasmcytosol Ref.4.

Tissue specificity

Expressed in roots, cotyledons, leaves, stems, cauline leaves, stigma, sepals and petals. Ref.6

Disruption phenotype

Embryonic lethality due to arrest of embryogenesis at the preglobular stage when homozygous. Ref.6

Sequence similarities

Belongs to the pantothenate synthetase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 9.0. Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 310310Pantoate--beta-alanine ligase HAMAP-Rule MF_00158
PRO_0000128299

Regions

Nucleotide binding32 – 398ATP By similarity
Nucleotide binding175 – 1784ATP By similarity
Nucleotide binding212 – 2154ATP By similarity

Sites

Active site391Proton donor By similarity
Binding site631Beta-alanine By similarity
Binding site631Pantoate By similarity
Binding site1811Pantoate By similarity

Experimental info

Mutagenesis1321E → A: Reduces allosteric properties. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9FKB3 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: AD07D927625AD1A6

FASTA31034,137
        10         20         30         40         50         60 
MEPEVIRDKD SMRKWSRAMR SQGKTIGLVP TMGYLHEGHL SLVRQSLALT DVTVVSIYVN 

        70         80         90        100        110        120 
PGQFSPTEDL STYPSDFSGD LTKLAALSGG KVVVFNPKNL YDYGGETKKI NDGGGNGGRV 

       130        140        150        160        170        180 
VSCVEEGGLG HETWIRVERL EKGFCGKSRP VFFRGVATIV TKLFNIVEPD VALFGKKDYQ 

       190        200        210        220        230        240 
QWRIIQRMVR DLNFGIEIVG SDIAREKDGL AMSSRNVRLS DEERQRALSI SRSLAMAKAS 

       250        260        270        280        290        300 
VAEGKTNCAE LKDMIIQQVV GSAGRVDYVE IVDQETLEGV EEIKSGVVIC VAAWFGTVRL 

       310 
IDNIEINVSL 

« Hide

References

« Hide 'large scale' references
[1]"Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence features of the regions of 1,367,185 bp covered by 19 physically assigned P1 and TAC clones."
Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N., Tabata S.
DNA Res. 5:203-216(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Pantothenate biosynthesis in higher plants."
Coxon K.M., Chakauya E., Ottenhof H.H., Whitney H.M., Blundell T.L., Abell C., Smith A.G.
Biochem. Soc. Trans. 33:743-746(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[5]"Molecular adaptation and allostery in plant pantothenate synthetases."
Jonczyk R., Genschel U.
J. Biol. Chem. 281:37435-37446(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, ALLOSTERIC PROPERTIES, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF GLU-132.
[6]"Pantothenate synthetase is essential but not limiting for pantothenate biosynthesis in Arabidopsis."
Jonczyk R., Ronconi S., Rychlik M., Genschel U.
Plant Mol. Biol. 66:1-14(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012242 Genomic DNA. Translation: BAB09437.1.
CP002688 Genomic DNA. Translation: AED95732.1.
AK175238 mRNA. Translation: BAD43001.1.
RefSeqNP_199695.1. NM_124261.3.
UniGeneAt.29821.

3D structure databases

ProteinModelPortalQ9FKB3.
SMRQ9FKB3. Positions 5-303.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9FKB3.
PRIDEQ9FKB3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G48840.1; AT5G48840.1; AT5G48840.
GeneID834942.
KEGGath:AT5G48840.

Organism-specific databases

TAIRAT5G48840.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
InParanoidQ9FKB3.
KOK01918.
OMAECPIVRE.
PhylomeDBQ9FKB3.

Enzyme and pathway databases

BioCycARA:AT5G48840-MONOMER.
MetaCyc:AT5G48840-MONOMER.
UniPathwayUPA00028; UER00005.

Gene expression databases

GenevestigatorQ9FKB3.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Other

PROQ9FKB3.

Entry information

Entry namePANC_ARATH
AccessionPrimary (citable) accession number: Q9FKB3
Secondary accession number(s): Q682X9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names