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Q4JXL9 (PANC_CORJK) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 55. 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:
Pantothenate synthetase

Short name=PS
EC=6.3.2.1
Alternative name(s):
Pantoate--beta-alanine ligase
Pantoate-activating enzyme
Gene names
Name:panC
Ordered Locus Names:jk0286
OrganismCorynebacterium jeikeium (strain K411) [Complete proteome] [HAMAP]
Taxonomic identifier306537 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate By similarity. HAMAP-Rule MF_00158

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 By similarity. HAMAP-Rule MF_00158

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity.

Sequence similarities

Belongs to the pantothenate synthetase family.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   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-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 306306Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305431

Regions

Nucleotide binding37 – 448ATP By similarity
Nucleotide binding155 – 1584ATP By similarity
Nucleotide binding192 – 1954ATP By similarity

Sites

Active site441Proton donor By similarity
Binding site691Beta-alanine By similarity
Binding site691Pantoate By similarity
Binding site1611Pantoate By similarity
Binding site1841ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4JXL9 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: A1A86774A8B87F15

FASTA30632,368
        10         20         30         40         50         60 
MTFTPGQAEV FTEIEKIGQL TRAMRKAGRP VALVPTMGAL HEGHLSLVQA AQQIPGALVV 

        70         80         90        100        110        120 
VSIFVNPLQF AEGEDLDAYP RTLDEDVAKL KAAGVDAVFA PSPREMYPNG PRTTIHPGEA 

       130        140        150        160        170        180 
GRILEGAHRP THFAGVLTVV NKLFTITHCD HAFFGEKDYQ QLLLIQQIVT DLNMEVQVHG 

       190        200        210        220        230        240 
VPIVREADGL AKSSRNVYLS DEERELALTL SAALTAGAFV AEQGPAAVLQ TAGSILDAAS 

       250        260        270        280        290        300 
GIDVDYLELR GTDLSDTPED GEARLLVAAR VGTTRLIDNV GVPLGTGFKG LDDGGEGSAP 


ADNAGE 

« Hide

References

[1]"Complete genome sequence and analysis of the multiresistant nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring bacterium of the human skin flora."
Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B., Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T., Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P., Puehler A.
J. Bacteriol. 187:4671-4682(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K411.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR931997 Genomic DNA. Translation: CAI36438.1.
RefSeqYP_250056.1. NC_007164.1.

3D structure databases

ProteinModelPortalQ4JXL9.
SMRQ4JXL9. Positions 2-286.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING306537.jk0286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI36438; CAI36438; jk0286.
GeneID3432855.
KEGGcjk:jk0286.
PATRIC21511428. VBICorJei31838_0296.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAPTHFAGM.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycCJEI306537:GJ8V-292-MONOMER.
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]
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_CORJK
AccessionPrimary (citable) accession number: Q4JXL9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: August 2, 2005
Last modified: June 11, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways