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Q5Z2U3 (PANC_NOCFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:NFA_4060
OrganismNocardia farcinica (strain IFM 10152) [Complete proteome] [HAMAP]
Taxonomic identifier247156 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeNocardia

Protein attributes

Sequence length318 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 – 318318Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000128250

Regions

Nucleotide binding44 – 518ATP By similarity
Nucleotide binding161 – 1644ATP By similarity
Nucleotide binding198 – 2014ATP By similarity

Sites

Active site511Proton donor By similarity
Binding site751Beta-alanine By similarity
Binding site751Pantoate By similarity
Binding site1671Pantoate By similarity
Binding site1901ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5Z2U3 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: F443D21E97FF5D68

FASTA31833,561
        10         20         30         40         50         60 
MIDPTLRGAY RPGQLTVHHD PAVLGSVAKA LRGVGRTVAL VPTMGALHQG HLQIVRQAKR 

        70         80         90        100        110        120 
TNQVVIVSIF VNPLQFGAGE DLDKYPRTLD ADVELLRAEG VELVFAPNAE QMYPDGPRTT 

       130        140        150        160        170        180 
VHPGPLGAEL EGASRPTHFA GMLTVVAKLL QIARPHQAFF GEKDYQQLTL IRQMVRDLNF 

       190        200        210        220        230        240 
DVRIVAVPTV RESDGLALSS RNRYLDAAQR ETALALSAAL SAGAHAGGLG AEGVLAAARA 

       250        260        270        280        290        300 
VLDATPGLDL DYLELRSSTL GPAPASGNAR LLVAAKVGTT RLIDNIAVTL GAPIDGHPNL 

       310 
DSQPEPAGTD PALLPPAR 

« Hide

References

[1]"The complete genomic sequence of Nocardia farcinica IFM 10152."
Ishikawa J., Yamashita A., Mikami Y., Hoshino Y., Kurita H., Hotta K., Shiba T., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 101:14925-14930(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IFM 10152.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006618 Genomic DNA. Translation: BAD55248.1.
RefSeqYP_116612.1. NC_006361.1.

3D structure databases

ProteinModelPortalQ5Z2U3.
SMRQ5Z2U3. Positions 9-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING247156.nfa4060.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD55248; BAD55248; NFA_4060.
GeneID3111359.
KEGGnfa:nfa4060.
PATRIC22730292. VBINocFar94200_0411.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
KOK01918.
OMAPTHFAGM.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycNFAR247156:GJ9T-418-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
InterProIPR004821. Cyt_trans-like.
IPR003721. Pantoate_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_NOCFA
AccessionPrimary (citable) accession number: Q5Z2U3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: November 23, 2004
Last modified: June 11, 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