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Reviewed, UniProtKB/Swiss-Prot Q6G456 (PANC_BARHE)

Last modified June 16, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: BH05120
OrganismBartonella henselae (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier38323 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm Potential.

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: 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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284Pantothenate synthetase HAMAP MF_00158
PRO_0000128206

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
Q6G456-1 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 12914B6A1302A413

FASTA28432,021
        10         20         30         40         50         60 
MRVLKTIPEV RQSITEERRL GFSIGLVPTM GALHNGHIAL VRRARAMCDR VLVSIFVNPK 

        70         80         90        100        110        120 
QFGPDEDFDK YPRDLKGDCA LLEEAGVEYL FTPSVEEMWP PGNETIVNVE KLSRMLIGKL 

       130        140        150        160        170        180 
RPGHFCGVTS VVAKLFNIVQ PDKAFFGEKD FQQILIVRRM VEDLAFPIEV VGVPVLREAD 

       190        200        210        220        230        240 
GVASSSRNQF LTLEDRKAAK IIPESGKAAE NLYRQGERSV DKLCKIVRDI LQQESRAIIE 

       250        260        270        280 
SIDLRDMETL SVVKGRLDKS AVLLLTVRFG EIRLIDQYIL QEKG 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

BX897699 Genomic DNA. Translation: CAF27320.1. Different initiation.

3D structure databases

ModBaseSearch...

Genome annotation databases

GenomeReviewsGene locus BH05120 in contig BX897699_GR.
KEGGbhe:BH05120.
NMPDRfig|283166.1.peg.476.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6G456.

Enzyme and pathway databases

BioCycBHEN283166:BH05120-MON.
BRENDA6.3.2.1. 277357.

Family and domain databases

HAMAPMF_00158.
[Tree]
InterProIPR004821. Cyt_trans_rel.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR21299:SF1. Pantoate_ligase. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_BARHE
AccessionPrimary (citable) accession number: Q6G456
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 2, 2007
Last modified: June 16, 2009
This is version 30 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents