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Q2N659 (PANC_ERYLH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 52. 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:ELI_13700
OrganismErythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]
Taxonomic identifier314225 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter

Protein attributes

Sequence length286 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 – 286286Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305442

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding188 – 1914ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1531Pantoate By similarity
Binding site1801ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2N659 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: FD489C796CA3A60D

FASTA28630,489
        10         20         30         40         50         60 
MQTIDRLDML RTSVAALRQG GGTVALVPTM GALHEGHLTL VREAAGRADH VVASIFVNPT 

        70         80         90        100        110        120 
QFGPNEDLDA YPRQLAEDCA MLEAEGVALV WAPTVEQMYP EGFASSISVS GVSEGLCGAD 

       130        140        150        160        170        180 
RPGHFDGVAT VVCKLFHQVL PDMAFFGEKD WQQLAVIRVM ARDLDLTRPH VAAIRGVATV 

       190        200        210        220        230        240 
REEDGLAMSS RNRYLSPEHR QAAAILPRAM KEAIGAIENG AAVAPTLASL EAALLQAGFD 

       250        260        270        280 
SVDYATLADA ANLQPLERLA MRPARLLVAA RIGGTRLIDN MAVGKV 

« Hide

References

[1]"Complete genome sequence of Erythrobacter litoralis HTCC2594."
Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC2594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000157 Genomic DNA. Translation: ABC64832.1.
RefSeqYP_459629.1. NC_007722.1.

3D structure databases

ProteinModelPortalQ2N659.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314225.ELI_13700.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC64832; ABC64832; ELI_13700.
GeneID3870692.
KEGGeli:ELI_13700.
PATRIC21862653. VBIEryLit102657_2737.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAPTHFAGM.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycELIT314225:GHLE-2787-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_ERYLH
AccessionPrimary (citable) accession number: Q2N659
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: February 7, 2006
Last modified: February 19, 2014
This is version 52 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