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B7HL54 (PANC_BACC7) 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:BCAH187_A1707
OrganismBacillus cereus (strain AH187) [Complete proteome] [HAMAP]
Taxonomic identifier405534 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length282 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 – 282282Pantothenate synthetase HAMAP MF_00158
PRO_1000118143

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
B7HL54 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: E127C01A4BBFDFE6

FASTA28231,981
        10         20         30         40         50         60 
MKIINTVQEM QQITNELRAS GKSIGFVPTM GYLHEGHATL LRKAREENEI VVLSVFVNPL 

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

       130        140        150        160        170        180 
RPGHFAGVAI VLMKLFNITL PTRAYFGMKD AQQVAVIEGF VADFNIPVTI VPVDIVREED 

       190        200        210        220        230        240 
GLAKSSRNVY LSPEEREEAL HLYRSLCIAK ERIETGERNA EIITTLVKEY IETYTKGTVD 

       250        260        270        280 
YADLYAYPSL QVVDKIEGRI ILAIAVKFDN VRLIDNITLT VK 

« Hide

References

[1]"Genome sequence of Bacillus cereus AH187."
Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B., Okstad O.A., Ravel J., Sutton G.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AH187.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001177 Genomic DNA. Translation: ACJ77754.1.
RefSeqYP_002337669.1. NC_011658.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB7HL54.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000094545; EBBACP00000090504; EBBACG00000094538.
GeneID7073679.
GenomeReviewsGene locus BCAH187_A1707 in contig CP001177_GR.
KEGGbcr:BCAH187_A1707.
PATRIC18828823. VBIBacCer120511_1885.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001451.
HOGENOMHBG428839.
OMAEMDGLAM.
ProtClustDBPRK00380.

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.
KOK01918.
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_BACC7
AccessionPrimary (citable) accession number: B7HL54
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 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