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Q1QKN4 (PANC_NITHX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 50. 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:Nham_2423
OrganismNitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]
Taxonomic identifier323097 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length283 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 – 283283Pantothenate synthetase HAMAP-Rule MF_00158
PRO_0000305496

Regions

Nucleotide binding34 – 418ATP By similarity
Nucleotide binding152 – 1554ATP By similarity
Nucleotide binding189 – 1924ATP By similarity

Sites

Active site411Proton donor By similarity
Binding site651Beta-alanine By similarity
Binding site651Pantoate By similarity
Binding site1581Pantoate By similarity
Binding site1811ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QKN4 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 9EEFC7454AC59D69

FASTA28330,951
        10         20         30         40         50         60 
MPRAPAIART LPSLRRALEG LRARRATVAL VPTMGALHDG HLALVRQAKR RASKVVVSIF 

        70         80         90        100        110        120 
VNPTQFAPHE DFGSYPRTWK ADMAKLAEAR VDLVWNPDVG TMYPPDFATR ILTEGPAMAG 

       130        140        150        160        170        180 
LEDRFRPHFF GGVATVVGKL FAQCRPDVAL FGQKDYQQFK VVTRMATDLD LGVKIIGVPI 

       190        200        210        220        230        240 
VRERDGLAMS SRNAYLSAEQ RAVAPTLHRV MKDAAKRLRN GDDLETVMAD GAGTIVDAGF 

       250        260        270        280 
ALDYFEARHA ETLAPVRSIK DGPVRLLVAA KIGTTRLIDN IGV 

« Hide

References

[1]"Complete sequence of chromosome of Nitrobacter hamburgensis X14."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: X14 / DSM 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000319 Genomic DNA. Translation: ABE63213.1.
RefSeqYP_577673.1. NC_007964.1.

3D structure databases

ProteinModelPortalQ1QKN4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323097.Nham_2423.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE63213; ABE63213; Nham_2423.
GeneID4030366.
KEGGnha:Nham_2423.
PATRIC22692654. VBINitHam61822_3336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0414.
HOGENOMHOG000175516.
KOK01918.
OMAHLGHITL.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK00380.

Enzyme and pathway databases

BioCycNHAM323097:GHP7-2463-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_NITHX
AccessionPrimary (citable) accession number: Q1QKN4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: May 16, 2006
Last modified: February 19, 2014
This is version 50 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