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B9LIH9 (PANC_CHLSY) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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:Chy400_2379
OrganismChloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl) [Complete proteome] [HAMAP]
Taxonomic identifier480224 [NCBI]
Taxonomic lineageBacteriaChloroflexiChloroflexalesChloroflexaceaeChloroflexus

Protein attributes

Sequence length281 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 – 281281Pantothenate synthetase HAMAP-Rule MF_00158
PRO_1000123406

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
B9LIH9 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: E7F3A49253D840A7

FASTA28131,012
        10         20         30         40         50         60 
MKVLHTVAEF RQARAAFDVL GFVPTMGYLH QGHLALVEQA RRECPAVAVS IFVNPTQFGP 

        70         80         90        100        110        120 
NEDYARYPRD TNRDLALLEA AGVDLVFIPS VEEMYPPGFG TYVIQPAADE VLEGAARPGH 

       130        140        150        160        170        180 
FRGVATVVCK LFNIVQPTKS YFGQKDAQQT VVVRQMVRDL NLPVEIVIVP TVREPDGLAL 

       190        200        210        220        230        240 
SSRNVYLNAE QRAAAPVLYR ALRTAAERYA AGERDAETLR AVMRSVLAGE PLARPDYVSV 

       250        260        270        280 
AHPLTLRELD RIGADGALLS MAVRFDQVRL IDNWLLEGEG K 

« Hide

References

[1]"Complete sequence of Chloroflexus sp. Y-400-fl."
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., Sims D., Kiss H., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Ovchinnikova G., Bryant D.A., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29364 / DSM 637 / Y-400-fl.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001364 Genomic DNA. Translation: ACM53773.1.
RefSeqYP_002570099.1. NC_012032.1.

3D structure databases

ProteinModelPortalB9LIH9.
SMRB9LIH9. Positions 1-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING480224.Chy400_2379.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM53773; ACM53773; Chy400_2379.
GeneID7402872.
KEGGchl:Chy400_2379.
PATRIC21424397. VBIChlSp61043_2487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAECPIVRE.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycCSP480224:GHIY-2413-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_CHLSY
AccessionPrimary (citable) accession number: B9LIH9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 35 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