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Q9RV66 (PANC_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. 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:DR_1164
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

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
Reference 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_0000128225

Regions

Nucleotide binding17 – 248ATP By similarity
Nucleotide binding134 – 1374ATP By similarity
Nucleotide binding176 – 1794ATP By similarity

Sites

Active site241Proton donor By similarity
Binding site481Beta-alanine By similarity
Binding site481Pantoate By similarity
Binding site1401Pantoate By similarity
Binding site1631ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9RV66 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 91112B0C2B9AEDA8

FASTA28130,118
        10         20         30         40         50         60 
MQTALASRGR VGLVPTMGFL HEGHATLIRR ARAECDVVVV SIFVNPMQFG PTEDLATYPR 

        70         80         90        100        110        120 
DLDRDLALAG AAGADFVFHP EAAAMYPAGF STRVEVSGVS EPLDGAARPG HFAGVATVVL 

       130        140        150        160        170        180 
KLLNIVQPER AYFGEKDWQQ LAVVRRLVAD LNLRSEIVGV PTVRADEEAA HAGLALSSRN 

       190        200        210        220        230        240 
SYLSPEQQRR ATVLSRALRA VQAAYAGGER DTGRLRQAGL DVLASEPELA LDYLVVVGPD 

       250        260        270        280 
LRDVPQLSDD PLNRVLIAGR LFGVRLIDNM PLSTAPVPAP A 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000513 Genomic DNA. Translation: AAF10737.1.
PIRG75430.
RefSeqNP_294888.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ9RV66.
SMRQ9RV66. Positions 8-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_1164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF10737; AAF10737; DR_1164.
GeneID1800443.
KEGGdra:DR_1164.
PATRIC21629922. VBIDeiRad64572_1362.

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAALHKGHQ.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycDRAD243230:GH46-1191-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_DEIRA
AccessionPrimary (citable) accession number: Q9RV66
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 87 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