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Q21U08 (PANC_ALBFT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. 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:Rfer_3034
OrganismAlbidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) (Rhodoferax ferrireducens) [Complete proteome] [HAMAP]
Taxonomic identifier338969 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeRhodoferax

Protein attributes

Sequence length282 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 – 282282Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305530

Regions

Nucleotide binding26 – 338ATP By similarity
Nucleotide binding144 – 1474ATP By similarity
Nucleotide binding181 – 1844ATP By similarity

Sites

Active site331Proton donor By similarity
Binding site571Beta-alanine By similarity
Binding site571Pantoate By similarity
Binding site1501Pantoate By similarity
Binding site1731ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21U08 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: AE4D94B60BD5C0EA

FASTA28231,072
        10         20         30         40         50         60 
MKIVRTIAEL RQHLSAYKHP AFVPTMGNLH EGHLSLLRQA KPLGDVLVAS IFVNRLQFLP 

        70         80         90        100        110        120 
HEDFDTYPRT WEADCQALQA AGCDVLFAPG EQELYPEPQT YRVQPPAELA DILEGHFRPG 

       130        140        150        160        170        180 
FFVGVSTVVM KLFACVQPRV AVFGQKDYQQ LMVIRGMVRQ FALPIAVLGV ATLRAADGLA 

       190        200        210        220        230        240 
LSSRNNYLTP LERAEAVHLS QSLQQMAKAL RAGTVDIAAL EQQAMVDLTA RGWQPDYLAA 

       250        260        270        280 
RRRADLQVPA ADEVAALVQN DGLVLLGAAR IGNTRLIDNL EV 

« Hide

References

[1]"Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio 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., Ivanova N., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-621 / DSM 15236 / T118.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000267 Genomic DNA. Translation: ABD70745.1.
RefSeqYP_524276.1. NC_007908.1.

3D structure databases

ProteinModelPortalQ21U08.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338969.Rfer_3034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD70745; ABD70745; Rfer_3034.
GeneID3961009.
KEGGrfr:Rfer_3034.
PATRIC23238817. VBIRhoFer131161_3404.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAHAGHMEL.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycAFER338969:GHU9-3073-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_ALBFT
AccessionPrimary (citable) accession number: Q21U08
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: April 18, 2006
Last modified: June 11, 2014
This is version 54 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