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Reviewed, UniProtKB/Swiss-Prot Q2IFU3 (PANC_ANADE)

Last modified February 9, 2010. Version 27. 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: Adeh_3681
OrganismAnaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]
Taxonomic identifier290397 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length289 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: 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 – 289289Pantothenate synthetase HAMAP MF_00158
PRO_0000305390

Regions

Nucleotide binding33 – 408ATP By similarity
Nucleotide binding157 – 1604ATP By similarity
Nucleotide binding194 – 1974ATP By similarity

Sites

Active site401Proton donor By similarity
Binding site701Beta-alanine By similarity
Binding site701Pantoate By similarity
Binding site1631Pantoate By similarity
Binding site1861ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2IFU3-1 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: F55FC51F1DA2F117

FASTA28930,882
        10         20         30         40         50         60 
MKTPELITDP AAWQARCTAA REAGTRIALV TTMGYLHEGH LSLMREARRR ADAGGRRGLA 

        70         80         90        100        110        120 
VGTIFVNPTQ FGPTEDLARY PRDLEGDLAK CAAAGLDAVL APSDPALMFA PGHETWVTVE 

       130        140        150        160        170        180 
RASQGLDGAS RPGHFRGVAT VVAKLFNLTR PHVALFGEKD WQQLAVIRAM VRDLAFGIEI 

       190        200        210        220        230        240 
VGMPIVREPD GLALSSRNAY LSPDERRRAL ALSGALAEAR EATARGERDA AALRAGARAR 

       250        260        270        280 
LEAAGGRVDY VELVHPETLA PVARAEPGTV LLLAASFGTT RLIDNGRLP 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000251 Genomic DNA. Translation: ABC83447.1.
RefSeqYP_466884.1.

3D structure databases

SMRQ2IFU3. Positions 5-288.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2IFU3.

Genome annotation databases

GeneID3886456.
GenomeReviewsGene locus Adeh_3681 in contig CP000251_GR.
KEGGade:Adeh_3681.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHBG428839.
OMAMPIQIIG.
PhylomeDBQ2IFU3.

Enzyme and pathway databases

BioCycADEH290397:ADEH_3681-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.
PANTHERPTHR21299:SF1. Pantoate_ligase. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_ANADE
AccessionPrimary (citable) accession number: Q2IFU3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 7, 2006
Last modified: February 9, 2010
This is version 27 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