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B5ES06 (PANC_ACIF5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 41. 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:Lferr_1446
OrganismAcidithiobacillus ferrooxidans (strain ATCC 53993) (Leptospirillum ferrooxidans (ATCC 53993)) [Complete proteome] [HAMAP]
Taxonomic identifier380394 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAcidithiobacillalesAcidithiobacillaceaeAcidithiobacillus

Protein attributes

Sequence length278 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 – 278278Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000118139

Regions

Nucleotide binding27 – 348ATP By similarity
Nucleotide binding147 – 1504ATP By similarity
Nucleotide binding184 – 1874ATP By similarity

Sites

Active site341Proton donor By similarity
Binding site581Beta-alanine By similarity
Binding site581Pantoate By similarity
Binding site1531Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
B5ES06 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: F2B5588544C6720E

FASTA27830,789
        10         20         30         40         50         60 
MAIFKDIAGL RQWRQSLHGT LALVPTMGNL HEGHLALVRL AANRAEHVLV SIYVNPLQFG 

        70         80         90        100        110        120 
PGEDFANYPR TLDQDLQRLH EAGCQTVFTP DDGLMYPRGR QDISIVMPPR SLSKVLCGAS 

       130        140        150        160        170        180 
RPGHFAGVCT VLSKLLHMVA PEILILGEKD YQQLRIVQQM VADLNLNVQV LPGPLQREAD 

       190        200        210        220        230        240 
GLAYSSRNIY LNLAERQVAP LLAETLFDLA RRSTNDAAVS DLAATGWERL ERAGFLPEYL 

       250        260        270 
ELRDAQTLQS LALPQPGARW FAAARLGQIR LIDNVIIS 

« Hide

References

[1]"Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Borole A.P.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 53993.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001132 Genomic DNA. Translation: ACH83677.1.
RefSeqYP_002219884.1. NC_011206.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING380394.Lferr_1446.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH83677; ACH83677; Lferr_1446.
GeneID6877420.
KEGGafe:Lferr_1446.
PATRIC20660482. VBIAciFer6930_1445.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAIHTIREL.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycAFER380394:GHE0-1471-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_ACIF5
AccessionPrimary (citable) accession number: B5ES06
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: October 14, 2008
Last modified: May 14, 2014
This is version 41 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