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O24035 (PANC_LOTJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Name:PANC
OrganismLotus japonicus (Lotus corniculatus var. japonicus)
Taxonomic identifier34305 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeLoteaeLotus

Protein attributes

Sequence length308 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158

Pathway

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

Subunit structure

Homodimer Potential.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Tissue specificity

Expressed at low levels in leaf and root. Ref.1

Sequence similarities

Belongs to the pantothenate synthetase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.8. Activity decreases sharply with increasing acidity and is null at pH 7. There is only a slight decrease toward higher pH. HAMAP-Rule MF_00158

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantoate-beta-alanine ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Propeptide21Removed; partial HAMAP-Rule MF_00158
PRO_0000023005
Chain3 – 308306Pantoate--beta-alanine ligase HAMAP-Rule MF_00158
PRO_0000023006

Sequences

Sequence LengthMass (Da)Tools
O24035 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 13344F2A8508D2D0

FASTA30834,240
        10         20         30         40         50         60 
MAPMVISDKD EMRKWSRSMR SQGKLIALVP TMGFLHEGHL SLVRDAHNHA DLVAVSIYVN 

        70         80         90        100        110        120 
PGQFSPTEDL SAYPSDFQGD LQKLMSVPGG VDVVFHPHNL YDYGGDGGDA VAECGGDGVV 

       130        140        150        160        170        180 
SCVDRRSGFG HETWVRAEKL EKPLCGKSRP VFFRGVATIV TKLFNIVEPD VAVFGKKDYQ 

       190        200        210        220        230        240 
QWKIIQRMVR DLDFSIKVIG SEVIREKDGL AMSSRNVYLS PEEREKAVSI NKSLFRAKSA 

       250        260        270        280        290        300 
AEDGQIHCEK LINLVVQSIT EAGGRIDYAE IVDQNNLEKV EWIKGPVVFC VSAWFGKARL 


IDNIEINL 

« Hide

References

[1]"The final step of pantothenate biosynthesis in higher plants: cloning and characterization of pantothenate synthetase from Lotus japonicus and Oryza sativum (rice)."
Genschel U., Powell C.A., Abell C., Smith A.G.
Biochem. J. 341:669-678(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-17, TISSUE SPECIFICITY.
Strain: cv. Gifu / B-129.
Tissue: Root nodule.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10252 mRNA. Translation: CAA71302.1.
UniGeneLja.12058.

3D structure databases

ProteinModelPortalO24035.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-9445.
BRENDA6.3.2.1. 3076.
UniPathwayUPA00028; UER00005.

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...

Entry information

Entry namePANC_LOTJA
AccessionPrimary (citable) accession number: O24035
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 2001
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 81 of the entry and version 3 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