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Reviewed, UniProtKB/Swiss-Prot B7JHQ7 (PANC_BACC0)

Last modified September 22, 2009. Version 7. 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: BCAH820_1634
OrganismBacillus cereus (strain AH820) [Complete proteome] [HAMAP]
Taxonomic identifier405535 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length282 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; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: 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 – 282282Pantothenate synthetase HAMAP MF_00158
PRO_1000118140

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
B7JHQ7-1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: C2081E04BCBD53D9

FASTA28231,963
        10         20         30         40         50         60 
MKIVTTVQEM QHITKELRAS GKSIGFVPTM GYLHEGHATL LRKAREENEI VVLSVFVNPL 

        70         80         90        100        110        120 
QFGPNEDLDR YPRDIDRDEN VAKENGVDYL FYPSVEEMYP AEQTTTVEVV KRTDVLCGKQ 

       130        140        150        160        170        180 
RPGHFAGVAT VLMKLFNITL PTRAYFGMKD AQQVAVIEGF VADFNIPVII VPVDIVREED 

       190        200        210        220        230        240 
GLAKSSRNVY LSQEERKEAP HLYRSLCMAK ERIEAGERNA EIITTLVKEY IETYTKGTVD 

       250        260        270        280 
YADLYAYPSL QVVDQIEGRI ILAIAVKFEN VRLIDNITLT VK 

« Hide

References

[1]"Genome sequence of Bacillus cereus AH820."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001283 Genomic DNA. Translation: ACK92271.1.
RefSeqYP_002450585.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7191073.
GenomeReviewsGene locus BCAH820_1634 in contig CP001283_GR.
KEGGbcu:BCAH820_1634.

Organism-specific databases

CMRSearch...

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_BACC0
AccessionPrimary (citable) accession number: B7JHQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: September 22, 2009
This is version 7 of the entry and version 1 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