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Q7UTQ8 (PANC_RHOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:RB3735
OrganismRhodopirellula baltica (strain SH1)
Taxonomic identifier243090 [NCBI]
Taxonomic lineageBacteriaPlanctomycetesPlanctomycetaciaPlanctomycetalesPlanctomycetaceaeRhodopirellula

Protein attributes

Sequence length283 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
Reference 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 – 283283Pantothenate synthetase HAMAP MF_00158
PRO_0000305531

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding150 – 1534ATP By similarity
Nucleotide binding187 – 1904ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1561Pantoate By similarity
Binding site1791ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7UTQ8 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 4A99472A7608B58E

FASTA28331,265
        10         20         30         40         50         60 
METFTSIDAM RAWCREKSRG GNTIGLVPTM GALHEGHLSL VHAAKKDCDH CVTSIFVNPT 

        70         80         90        100        110        120 
QFAANEDLDQ YPRPIEDDLA MLRDAGVEAV FMPTADEMYP GGPQTHATSV HPSAVAFPLE 

       130        140        150        160        170        180 
GVHRPEHFVG VATVVMKLFQ AAPSDRAFFG RKDLQQLCVI EHMVRDLNLP IEIVPCDIVR 

       190        200        210        220        230        240 
EPDGLAMSSR NRYLSDDQRQ RALCISKSLN QVEQAFLEGN HDPKQLESIM ADHLSPCDSV 

       250        260        270        280 
DYAVVVDRQT LLPISEITQN AVALVAVRVG VTRLIDNREL IVA 

« Hide

References

[1]"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1."
Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R.
Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed: 12835416] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SH1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX294139 Genomic DNA. Translation: CAD73378.1.
RefSeqNP_865693.1. NC_005027.1.

3D structure databases

HSSPHSSP built from PDB template 2A84 based on UniProtKB P0A5R0.
ProteinModelPortalQ7UTQ8.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1796897.
GenomeReviewsGene locus RB3735 in contig BX119912_GR.
KEGGrba:RB3735.
NMPDRfig|243090.1.peg.2033.
PATRIC23244907. VBIRhoBal59814_1737.

Phylogenomic databases

HOGENOMHBG428839.
OMAEMDGLAM.
PhylomeDBQ7UTQ8.

Enzyme and pathway databases

BioCycPSP117:RB3735-MONOMER.

Family and domain databases

HAMAPMF_00158. PanC.
[Tree]
InterProIPR003721. 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]
TIGRFAMsTIGR00018. PanC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_RHOBA
AccessionPrimary (citable) accession number: Q7UTQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 46 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