Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9FKB3

- PANC_ARATH

UniProt

Q9FKB3 - PANC_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pantoate--beta-alanine ligase

Gene

At5g48840

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the condensation of pantoate with beta-alanine to form pantothenate. Essential for panthotenate biosynthesis.2 Publications

Catalytic activityi

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate.1 Publication

Enzyme regulationi

Enzyme kinetics do not match Michaelis-Menten kinetics, suggesting allosteric behavior. Inhibited by high pantoate levels.1 Publication

pH dependencei

Optimum pH is 9.0.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei39 – 391Proton donorBy similarity
Binding sitei63 – 631Beta-alanineBy similarity
Binding sitei63 – 631PantoateBy similarity
Binding sitei181 – 1811PantoateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 398ATPBy similarity
Nucleotide bindingi175 – 1784ATPBy similarity
Nucleotide bindingi212 – 2154ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. pantoate-beta-alanine ligase activity Source: TAIR
  3. protein homodimerization activity Source: TAIR

GO - Biological processi

  1. embryo development ending in seed dormancy Source: TAIR
  2. pantothenate biosynthetic process Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pantothenate biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G48840-MONOMER.
MetaCyc:AT5G48840-MONOMER.
UniPathwayiUPA00028; UER00005.

Names & Taxonomyi

Protein namesi
Recommended name:
Pantoate--beta-alanine ligase (EC:6.3.2.1)
Alternative name(s):
Pantoate-activating enzyme
Pantothenate synthetase
Gene namesi
Ordered Locus Names:At5g48840
ORF Names:K24G6.18
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 5

Organism-specific databases

TAIRiAT5G48840.

Subcellular locationi

Cytoplasmcytosol 1 Publication

GO - Cellular componenti

  1. cytosol Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality due to arrest of embryogenesis at the preglobular stage when homozygous.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi132 – 1321E → A: Reduces allosteric properties. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 310310Pantoate--beta-alanine ligasePRO_0000128299Add
BLAST

Proteomic databases

PaxDbiQ9FKB3.
PRIDEiQ9FKB3.

Expressioni

Tissue specificityi

Expressed in roots, cotyledons, leaves, stems, cauline leaves, stigma, sepals and petals.1 Publication

Gene expression databases

GenevestigatoriQ9FKB3.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9FKB3.
SMRiQ9FKB3. Positions 5-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the pantothenate synthetase family.Curated

Phylogenomic databases

eggNOGiCOG0414.
HOGENOMiHOG000175516.
InParanoidiQ9FKB3.
KOiK01918.
OMAiECPIVRE.
PhylomeDBiQ9FKB3.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00158. PanC.
InterProiIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERiPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamiPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00018. panC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9FKB3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEPEVIRDKD SMRKWSRAMR SQGKTIGLVP TMGYLHEGHL SLVRQSLALT
60 70 80 90 100
DVTVVSIYVN PGQFSPTEDL STYPSDFSGD LTKLAALSGG KVVVFNPKNL
110 120 130 140 150
YDYGGETKKI NDGGGNGGRV VSCVEEGGLG HETWIRVERL EKGFCGKSRP
160 170 180 190 200
VFFRGVATIV TKLFNIVEPD VALFGKKDYQ QWRIIQRMVR DLNFGIEIVG
210 220 230 240 250
SDIAREKDGL AMSSRNVRLS DEERQRALSI SRSLAMAKAS VAEGKTNCAE
260 270 280 290 300
LKDMIIQQVV GSAGRVDYVE IVDQETLEGV EEIKSGVVIC VAAWFGTVRL
310
IDNIEINVSL
Length:310
Mass (Da):34,137
Last modified:March 1, 2001 - v1
Checksum:iAD07D927625AD1A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012242 Genomic DNA. Translation: BAB09437.1.
CP002688 Genomic DNA. Translation: AED95732.1.
AK175238 mRNA. Translation: BAD43001.1.
RefSeqiNP_199695.1. NM_124261.3.
UniGeneiAt.29821.

Genome annotation databases

EnsemblPlantsiAT5G48840.1; AT5G48840.1; AT5G48840.
GeneIDi834942.
KEGGiath:AT5G48840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB012242 Genomic DNA. Translation: BAB09437.1 .
CP002688 Genomic DNA. Translation: AED95732.1 .
AK175238 mRNA. Translation: BAD43001.1 .
RefSeqi NP_199695.1. NM_124261.3.
UniGenei At.29821.

3D structure databases

ProteinModelPortali Q9FKB3.
SMRi Q9FKB3. Positions 5-303.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q9FKB3.
PRIDEi Q9FKB3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT5G48840.1 ; AT5G48840.1 ; AT5G48840 .
GeneIDi 834942.
KEGGi ath:AT5G48840.

Organism-specific databases

TAIRi AT5G48840.

Phylogenomic databases

eggNOGi COG0414.
HOGENOMi HOG000175516.
InParanoidi Q9FKB3.
KOi K01918.
OMAi ECPIVRE.
PhylomeDBi Q9FKB3.

Enzyme and pathway databases

UniPathwayi UPA00028 ; UER00005 .
BioCyci ARA:AT5G48840-MONOMER.
MetaCyc:AT5G48840-MONOMER.

Miscellaneous databases

PROi Q9FKB3.

Gene expression databases

Genevestigatori Q9FKB3.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00158. PanC.
InterProi IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
PANTHERi PTHR21299:SF1. PTHR21299:SF1. 1 hit.
Pfami PF02569. Pantoate_ligase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00018. panC. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiPANC_ARATH
AccessioniPrimary (citable) accession number: Q9FKB3
Secondary accession number(s): Q682X9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2002
Last sequence update: March 1, 2001
Last modified: October 1, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3