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B6YS28 (PANC_AZOPC) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 22. 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:CFPG_737
OrganismAzobacteroides pseudotrichonymphae genomovar. CFP2 [Complete proteome] [HAMAP]
Taxonomic identifier511995 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesCandidatus Azobacteroides

Protein attributes

Sequence length280 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 – 280280Pantothenate synthetase HAMAP MF_00158
PRO_1000097029

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding148 – 1514ATP By similarity
Nucleotide binding185 – 1884ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1541Pantoate By similarity
Binding site1771ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B6YS28 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: 84D45C25AF00A5C0

FASTA28032,038
        10         20         30         40         50         60 
MEIIKTVVEL QTALLKIREQ NKSIGFVPTM GALHRGHIEL VKQSVVENTI SIVSIFVNPT 

        70         80         90        100        110        120 
QFNDKNDLLK YPRTLNADCK LLLQETNNHF VFAPSVEEIY SETNIQQFKF GHLETVMEGK 

       130        140        150        160        170        180 
LRPGHFNGVA QVVSRLFKIV KPNCAYFGEK DFQQLTIIRT LVRLLNLNVK IIPHPTVREP 

       190        200        210        220        230        240 
NGLALSSRNI HLTPKQKKNA GMIFKTLSKS RKEKNILSIQ ELKQKTINKI NCIPDFRVEY 

       250        260        270        280 
FDLVDGNTLQ SITDWKDTKY IVGCIAVYIG EVRLIDNITY 

« Hide

References

[1]"Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT protist cells in termite gut."
Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T., Sakaki Y., Toyoda A., Hattori M., Ohkuma M.
Science 322:1108-1109(2008) [PubMed: 19008447] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010656 Genomic DNA. Translation: BAG84000.1.
RefSeqYP_002309411.1. NC_011565.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB6YS28.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7039808.
GenomeReviewsGene locus CFPG_737 in contig AP010656_GR.
KEGGaps:CFPG_737.
PATRIC31963512. VBICanAzo57536_1109.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG428839.
OMANIVQPDK.
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_AZOPC
AccessionPrimary (citable) accession number: B6YS28
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 20, 2009
Last modified: January 25, 2012
This is version 22 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