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A8M8F3 (PANC_SALAI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:Sare_4718
OrganismSalinispora arenicola (strain CNS-205) [Complete proteome] [HAMAP]
Taxonomic identifier391037 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

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_1000076864

Regions

Nucleotide binding28 – 358ATP By similarity
Nucleotide binding146 – 1494ATP By similarity
Nucleotide binding183 – 1864ATP By similarity

Sites

Active site351Proton donor By similarity
Binding site591Beta-alanine By similarity
Binding site591Pantoate By similarity
Binding site1521Pantoate By similarity
Binding site1751ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A8M8F3 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: DE5C2C5007F24724

FASTA28230,023
        10         20         30         40         50         60 
MTELVHTRAE LAAARDGLTG TVGVVMTMGA LHSGHETLLR AARERADHVL VTIFVNPLQF 

        70         80         90        100        110        120 
GPDEDFNRYP RTLDVDLEIC RRAGVAVVFA PVVTELYPEG KPRVWVAPGQ LGEELEGQSR 

       130        140        150        160        170        180 
PGFFHGVLTV VLKLLHVTRP DLAFFGEKDY QQLTLVRRMV GDLDVPVEIV GVPTVREPDG 

       190        200        210        220        230        240 
LALSSRNRYL SPDERAAALS LSGALRAGAA AAAVGADAGA VLAAAHAAFE SGPSGARLDY 

       250        260        270        280 
LVLTDSDLEP GPTAGPARML VAAWVGTTRL IDNMSVQLAP YS 

« Hide

References

[1]"Complete sequence of Salinispora arenicola CNS-205."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K. expand/collapse author list , Jenkins C., Udwary D., Xiang L., Gontang E., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CNS-205.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000850 Genomic DNA. Translation: ABW00472.1.
RefSeqYP_001539462.1. NC_009953.1.

3D structure databases

ProteinModelPortalA8M8F3.
SMRA8M8F3. Positions 3-281.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8M8F3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5706020.
GenomeReviewsGene locus Sare_4718 in contig CP000850_GR.
KEGGsaq:Sare_4718.
PATRIC23438056. VBISalAre38676_4769.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG428839.
OMAEDFGSYP.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycSARE391037:SARE_4718-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_SALAI
AccessionPrimary (citable) accession number: A8M8F3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 4, 2007
Last modified: January 25, 2012
This is version 30 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