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C4L6Q1 (PANC_EXISA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 33. 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:EAT1b_3016
OrganismExiguobacterium sp. (strain ATCC BAA-1283 / AT1b) [Complete proteome] [HAMAP]
Taxonomic identifier360911 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillales Family XII. Incertae SedisExiguobacterium

Protein attributes

Sequence length276 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 – 276276Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000203491

Regions

Nucleotide binding26 – 338ATP By similarity
Nucleotide binding142 – 1454ATP By similarity
Nucleotide binding179 – 1824ATP By similarity

Sites

Active site331Proton donor By similarity
Binding site571Beta-alanine By similarity
Binding site571Pantoate By similarity
Binding site1481Pantoate By similarity
Binding site1711ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
C4L6Q1 [UniParc].

Last modified July 7, 2009. Version 1.
Checksum: BE42EC284BFDAA46

FASTA27631,205
        10         20         30         40         50         60 
MRIVSTVEEL RSALPMDQTI GFVPTMGYLH EGHMSLVENA RRENDVVVMS IFVNPTQFGP 

        70         80         90        100        110        120 
NEDLDRYPRD FERDEKLARE AGVDVLFYPT TETMYPLDMA RVTVRHGADV LCGASRPGHF 

       130        140        150        160        170        180 
DGVLTIVSKL FNLVQPTRAY FGLKDAQQVA LIEGYVRDYF VPVEIRRCPI IREETGLAKS 

       190        200        210        220        230        240 
SRNVYLSDIE TVEASRIFSA LTMAREALDA GQQVDEVKRQ LIERLDEIPN SQIDYVELVD 

       250        260        270 
YPTLGAVSSD STELLLAVAI QFERARLIDN VIWKKG 

« Hide

References

[1]"Complete sequence of Exiguobacterium sp. AT1b."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G. expand/collapse author list , Ramaley R.F., Rodrigues D.F., Vishnivetskaya T.A., Kathariou S., Tiedje J.M., Richardson P.
Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1283 / AT1b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001615 Genomic DNA. Translation: ACQ71930.1.
RefSeqYP_002887375.1. NC_012673.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360911.EAT1b_3016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ71930; ACQ71930; EAT1b_3016.
GeneID7868620.
KEGGeat:EAT1b_3016.
PATRIC21881290. VBIExiSp39724_2991.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAFFGMKDA.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycESP360911:GI4R-3114-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]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANC_EXISA
AccessionPrimary (citable) accession number: C4L6Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 7, 2009
Last modified: May 14, 2014
This is version 33 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