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Reviewed, UniProtKB/Swiss-Prot A6L4C3 (PANC_BACV8)

Last modified November 3, 2009. Version 18. 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: BVU_2898
OrganismBacteroides vulgatus (strain ATCC 8482 / DSM 1447 / NCTC 11154) [Complete proteome] [HAMAP]
Taxonomic identifier435590 [NCBI]
Taxonomic lineageBacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

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Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Subcellular location

Cytoplasm Potential.

Miscellaneous

The reaction proceeds by a bi uni uni bi ping pong mechanism By similarity.

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_0000305401

Regions

Nucleotide binding30 – 378ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding185 – 1884ATP By similarity

Sites

Active site371Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1531Pantoate By similarity
Binding site1771ATP; via amide nitrogen and carbonyl oxygen By similarity

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Sequences

Sequence LengthMass (Da)Tools
A6L4C3-1 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: AAD88717A66A8E15

FASTA28231,338
        10         20         30         40         50         60 
MKLVQTIKEL QSELDALRSE GKTIGLVPTM GALHAGHASL VKRAVAENDV VVVSDFVNPT 

        70         80         90        100        110        120 
QFNDKNDLAK YPRTLDADCE LLEKVGAAFV FAPSVEEIYP EPDTRQFSYA PLDTVMEGRF 

       130        140        150        160        170        180 
RPGHFNGVCQ IVSKLFMIVN PTRAYFGEKD FQQLAIIREM VKQIGFNGLE IVGCPIVREE 

       190        200        210        220        230        240 
DGLALSSRNA RLSAVEREYA LNISQTLFKS CTFAKSHPVA ETQKFVEDAI AAAPGLRLEY 

       250        260        270        280 
FEIVDGTTLQ KITDWEDTDY AVGCITVFCG EVRLIDNIKY KG

« Hide

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References

[1]"Evolution of symbiotic bacteria in the distal human intestine."
Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C., Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H., Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K., Knight R.D., Gordon J.I.
PLoS Biol. 5:1574-1586(2007) [PubMed: 17579514] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000139 Genomic DNA. Translation: ABR40537.1.
RefSeqYP_001300159.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA6L4C3.

Genome annotation databases

GeneID5303859.
GenomeReviewsGene locus BVU_2898 in contig CP000139_GR.
KEGGbvu:BVU_2898.
NMPDRfig|435590.6.peg.2715.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAYRAYFGQ.

Family and domain databases

HAMAPMF_00158.
[Tree]
InterProIPR003721. Pantoate_ligase.
[Graphical view]
PANTHERPTHR21299:SF1. Pantoate_ligase. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

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Entry information

Entry namePANC_BACV8
AccessionPrimary (citable) accession number: A6L4C3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: July 24, 2007
Last modified: November 3, 2009
This is version 18 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