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Reviewed, UniProtKB/Swiss-Prot B7HHU4 (PANC_BACC4)

Last modified February 9, 2010. Version 10. 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

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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: BCB4264_A1596
OrganismBacillus cereus (strain B4264) [Complete proteome] [HAMAP]
Taxonomic identifier405532 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

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Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Pantothenate synthetase HAMAP MF_00158
PRO_1000118142

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

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Sequences

Sequence LengthMass (Da)Tools
B7HHU4-1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: FDEB6289AA630E32

FASTA28231,905
        10         20         30         40         50         60 
MKIVTTVQEM QQITSELRAS GKSIGFVPTM GYLHEGHATL LRKAREENEI VVLSVFVNPL 

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

       130        140        150        160        170        180 
RPGHFAGVAT VLMKLFNITV PTRAYFGMKD AQQVAVIEGF VTDFNIPVTI VPVDIVREED 

       190        200        210        220        230        240 
GLAKSSRNVY LSQDEREEAL HLYRSLCIAK ERIEAGERNP EIITNLVKDY IETHTKGTVD 

       250        260        270        280 
YADLYAYPSL TMVEKVEGRI ILAIAVKFEN VRLIDNITLT VK

« Hide

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References

[1]"Genome sequence of Bacillus cereus B4264."
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].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001176 Genomic DNA. Translation: ACK64054.1.
RefSeqYP_002366321.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7097070.
GenomeReviewsGene locus BCB4264_A1596 in contig CP001176_GR.
KEGGbcb:BCB4264_A1596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG428839.

Family and domain databases

HAMAPMF_00158. PanC.
[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...

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Entry information

Entry namePANC_BACC4
AccessionPrimary (citable) accession number: B7HHU4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: February 9, 2010
This is version 10 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)

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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