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B6JPA5 (PANC_HELP2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. 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:HPP12_0006
OrganismHelicobacter pylori (strain P12) [Complete proteome] [HAMAP]
Taxonomic identifier570508 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length276 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 – 276276Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000097072

Regions

Nucleotide binding27 – 348ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site341Proton donor By similarity
Binding site581Beta-alanine By similarity
Binding site581Pantoate By similarity
Binding site1531Pantoate By similarity
Binding site1761ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B6JPA5 [UniParc].

Last modified December 16, 2008. Version 1.
Checksum: 3073FA57C23DB323

FASTA27631,201
        10         20         30         40         50         60 
MRVLETIAVL REYRKSLKES VGFVPTMGAL HRGHQSLIER SLKENSHTIV SVFVNPTQFG 

        70         80         90        100        110        120 
ANEDFSAYPR PLEKDLALCE KLGVSAVFVP KVSEMYPYEI EQRLKLYAPT FLSHSLEGAV 

       130        140        150        160        170        180 
RHGHFDGVVQ VVLRLFHLVN PTRAYFGKKD AQQLLIIEHL VKDLLLDIEI APCEIARDSD 

       190        200        210        220        230        240 
HLALSSRNVY LNATERKQAL AIPKALENIK QAIDKGEKAC EKLKKLGLEI LETLEVDYLE 

       250        260        270 
FCNHKLEPLK TIEPANTLVL VAARVGKTRL LDNLWV 

« Hide

References

[1]"The complete genome sequence of Helicobacter pylori strain P12."
Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: P12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001217 Genomic DNA. Translation: ACJ07166.1.
RefSeqYP_002300646.1. NC_011498.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING570508.HPP12_0006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ07166; ACJ07166; HPP12_0006.
GeneID7010369.
KEGGhpp:HPP12_0006.
PATRIC20607905. VBIHelPyl2824_0006.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175517.
KOK01918.
OMAHAGHMEL.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycHPYL570508:GJ8D-6-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_HELP2
AccessionPrimary (citable) accession number: B6JPA5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: December 16, 2008
Last modified: May 14, 2014
This is version 36 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