Skip Header

Contribute Send feedback
Read comments (?) or add your own

B4SDX5 (PANC_PELPB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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:Ppha_0667
OrganismPelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1) [Complete proteome] [HAMAP]
Taxonomic identifier324925 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobium/Pelodictyon groupPelodictyon

Protein attributes

Sequence length283 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 MF_00158

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP MF_00158

Subcellular location

Cytoplasm Potential HAMAP MF_00158.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity. HAMAP MF_00158

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-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 283283Pantothenate synthetase HAMAP MF_00158
PRO_1000097084

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1531Pantoate By similarity
Binding site1761ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B4SDX5 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 319830FF1CC175F8

FASTA28331,409
        10         20         30         40         50         60 
MQIITEPRQM QAIAEKLRLN RQFIGVVMTM GALHEGHLSL IKLARQSAGT VILTIFVNPS 

        70         80         90        100        110        120 
QFGANEDLHQ YPRPFEQDVA LATAAEVDYL FAPEAGTIYP ENHQTTLQCG ALGERLEGER 

       130        140        150        160        170        180 
RPGHFNGVAT IVTKLLHITK PHIAIFGEKD AQQLAVIRRM VEDLNLDVKI IAAPIIREEN 

       190        200        210        220        230        240 
GLAVSSRNIY LSNTERSTAG ILYQGICHAE KSIAEQKKNL SVIAAEIEQM IASTPGWRPD 

       250        260        270        280 
YVVFVDEERF EPAEIAEEGK EYRLLLAAYA GKVRLIDNGK IVA 

« Hide

References

[1]"Complete sequence of Pelodictyon phaeoclathratiforme BU-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F. expand/collapse author list , Overmann J., Bryant D.A., Richardson P.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 5477 / BU-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001110 Genomic DNA. Translation: ACF42966.1.
RefSeqYP_002017583.1. NC_011060.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB4SDX5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6461575.
GenomeReviewsGene locus Ppha_0667 in contig CP001110_GR.
KEGGpph:Ppha_0667.
PATRIC22901768. VBIPelPha134556_0676.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG428839.
OMALNMPIQI.
ProtClustDBPRK00380.

Family and domain databases

HAMAPMF_00158. PanC.
[Tree]
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01918.
PANTHERPTHR21299:SF1. Pantoate_ligase. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. PanC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_PELPB
AccessionPrimary (citable) accession number: B4SDX5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families