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Q0C347 (PANC_HYPNA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:HNE_1126
OrganismHyphomonas neptunium (strain ATCC 15444) [Complete proteome] [HAMAP]
Taxonomic identifier228405 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesHyphomonadaceaeHyphomonas

Protein attributes

Sequence length293 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 – 293293Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305467

Regions

Nucleotide binding38 – 458ATP By similarity
Nucleotide binding155 – 1584ATP By similarity
Nucleotide binding192 – 1954ATP By similarity

Sites

Active site451Proton donor By similarity
Binding site691Beta-alanine By similarity
Binding site691Pantoate By similarity
Binding site1611Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0C347 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 448A1FA1C09D5C29

FASTA29332,189
        10         20         30         40         50         60 
MNSTKENPVE IIRTRNELQA RVRAWKQAGE TVGFVPTMGA LHEGHLSLIE KAQEKVTRTV 

        70         80         90        100        110        120 
ASIFVNPAQF APGEDFDTYP RREGEDIAKL ASVNCDAVYL PTVAEMYPEG SVTNVRVESL 

       130        140        150        160        170        180 
SDLLDGIYRP HFFYGVATVV ARLFLHAQPD VAVFGEKDYQ QLQVIRRMVR DLGFPIEIIG 

       190        200        210        220        230        240 
GATRRDADGL AQSSRNLYLS PDERRAAGAI YSAMHRAASR MALGTLPSEA LKEAEGYILT 

       250        260        270        280        290 
AGFRKIDYVT LVDPATLQAL PADTPLEDGA AARLLAAAWI GKTRLIDNIS VTR 

« Hide

References

[1]"Comparative genomic evidence for a close relationship between the dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter crescentus."
Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G., Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D., Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R., Brinkac L.M. expand/collapse author list , Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G., Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N., Ward N.L.
J. Bacteriol. 188:6841-6850(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15444.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000158 Genomic DNA. Translation: ABI76807.1.
RefSeqYP_759846.1. NC_008358.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING228405.HNE_1126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI76807; ABI76807; HNE_1126.
GeneID4287761.
KEGGhne:HNE_1126.
PATRIC32215057. VBIHypNep17450_1126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAIRELRAW.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycHNEP228405:GI69-1126-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_HYPNA
AccessionPrimary (citable) accession number: Q0C347
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 53 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