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Q82Y17 (PANC_NITEU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:NE0073
OrganismNitrosomonas europaea (strain ATCC 19718 / NBRC 14298) [Complete proteome] [HAMAP]
Taxonomic identifier228410 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length277 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-Rule MF_00158

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_00158

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00158

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_00158.

Miscellaneous

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

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-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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 277277Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128249

Regions

Nucleotide binding26 – 338ATP By similarity
Nucleotide binding143 – 1464ATP By similarity
Nucleotide binding180 – 1834ATP By similarity

Sites

Active site331Proton donor By similarity
Binding site571Beta-alanine By similarity
Binding site571Pantoate By similarity
Binding site1491Pantoate By similarity
Binding site1721ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q82Y17 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8DA15A1056C92096

FASTA27731,131
        10         20         30         40         50         60 
MEIITDIAPL RARLRHEASV AFVPTMGNLH AGHLSLVRIA QKHASCSVVS IFVNRLQFAP 

        70         80         90        100        110        120 
HEDFDRYPRT WSDDCRLLEE QGADIVFMPD EKTLYPVPQE FQLLLPPVAD TLEGACRPGF 

       130        140        150        160        170        180 
FRGVTTVVLK LFNIVQPHIA VFGEKDYQQL QVVHRMVDQL NLPVEIIAGE TVRDEDGLAL 

       190        200        210        220        230        240 
SSRNNYLDAT QRQEAGELAH HLKQIRDSIA SGERDFPLLE QLAAEKLSKR GWVVDYVAVR 

       250        260        270 
QQHTLLPVAA SDSSLVILGA AWLNQTRLID NFLLTLP 

« Hide

References

[1]"Complete genome sequence of the ammonia-oxidizing bacterium and obligate chemolithoautotroph Nitrosomonas europaea."
Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L., Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A., Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.
J. Bacteriol. 185:2759-2773(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 19718 / NBRC 14298.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL954747 Genomic DNA. Translation: CAD83984.1.
RefSeqNP_840174.1. NC_004757.1.

3D structure databases

ProteinModelPortalQ82Y17.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228410.NE0073.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD83984; CAD83984; NE0073.
GeneID1083596.
KEGGneu:NE0073.
PATRIC22710927. VBINitEur56163_0080.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAQKDAQQF.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycNEUR228410:GJNO-83-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_NITEU
AccessionPrimary (citable) accession number: Q82Y17
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: June 1, 2003
Last modified: February 19, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways