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A3PF80 (PANCY_PROM0) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 52. 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:
Bifunctional pantoate ligase/cytidylate kinase

Including the following 2 domains:

  1. Pantothenate synthetase
    Short name=PS
    EC=6.3.2.1
    Alternative name(s):
    Pantoate--beta-alanine ligase
    Pantoate-activating enzyme
  2. Cytidylate kinase
    Short name=CK
    EC=2.7.4.14
    Alternative name(s):
    Cytidine monophosphate kinase
    Short name=CMP kinase
Gene names
Name:panC/cmk
Ordered Locus Names:P9301_17821
OrganismProchlorococcus marinus (strain MIT 9301) [Complete proteome] [HAMAP]
Taxonomic identifier167546 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length510 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_01349

Displays a CMP kinase activity By similarity. HAMAP-Rule MF_01349

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_01349

ATP + (d)CMP = ADP + (d)CDP. HAMAP-Rule MF_01349

Pathway

Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1. HAMAP-Rule MF_01349

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01349.

Sequence similarities

In the N-terminal section; belongs to the pantothenate synthetase family.

In the C-terminal section; belongs to the cytidylate kinase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPantothenate biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Ligase
Transferase
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processpantothenate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

pyrimidine nucleotide metabolic 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-HAMAP

cytidylate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

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 – 510510Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_01349
PRO_0000333297

Regions

Nucleotide binding29 – 368ATP By similarity
Nucleotide binding150 – 1534ATP By similarity
Nucleotide binding187 – 1904ATP By similarity
Region1 – 276276Pantoate--beta-alanine ligase HAMAP-Rule MF_01349
Region277 – 510234Cytidylate kinase HAMAP-Rule MF_01349

Sites

Active site361Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1561Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
A3PF80 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: E82DF93842EDC030

FASTA51058,445
        10         20         30         40         50         60 
MKKVIIRKTE EIENWRRNIN SEINFIPTMG NLHDGHIKLI STAKNDNSNV NLVSIFINPL 

        70         80         90        100        110        120 
QFDNKLDLEN YPQTIDNDIK ISFSNGADAI FIPSYEDIYP PNNKNIKFLK APKELSSALC 

       130        140        150        160        170        180 
GLNRIGHFDG VCTVVYRLLN LIKPKNLYLG EKDWQQLLIL KNLVLRKNLN VAIRSIPTQR 

       190        200        210        220        230        240 
DFDGIPLSSR NVHLSKNERK LISFFSSELL EAKKIFQQDK KINLNQIIKK LSAKKISVEY 

       250        260        270        280        290        300 
LEHLHPHTLQ KARPEDNISL LAGAIRCGET RLIDHVFLMK RRPIIAIDGP AGSGKSTVTK 

       310        320        330        340        350        360 
LIAKKLNLLY LDTGAMYRAL SWLIIKESVD YKIEKKLQNI LKDISIFFKS NTNSHQDVYV 

       370        380        390        400        410        420 
NNYCVTKEIR SQKISSIVSK ISSIKEVRKF LVAEQRKIGE SGGLVAEGRD IGTTVFPHAE 

       430        440        450        460        470        480 
LKIFLTASID ERAKRRKYDK NSKDSQEIDL YTLKELIKKR DFEDSNREIS PLIKANDAIE 

       490        500        510 
IITDGYTIDE VVDKIIDLYN DRIPKETEIK 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000576 Genomic DNA. Translation: ABO18405.1.
RefSeqYP_001092006.1. NC_009091.1.

3D structure databases

ProteinModelPortalA3PF80.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167546.P9301_17821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO18405; ABO18405; P9301_17821.
GeneID4911848.
KEGGpmg:P9301_17821.
PATRIC22997073. VBIProMar103344_1706.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0283.
HOGENOMHOG000233355.
KOK13799.
OMALGEKDWQ.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycPMAR167546:GH1Y-1831-MONOMER.
UniPathwayUPA00028; UER00005.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00158. PanC.
MF_00238. Cytidyl_kinase_type1.
MF_01349. PanCY.
InterProIPR003136. Cytidylate_kin.
IPR011994. Cytidylate_kinase_dom.
IPR027417. P-loop_NTPase.
IPR003721. Pantoate_ligase.
IPR024894. Pantoate_ligase/cytidylate_kin.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF2. PTHR21299:SF2. 1 hit.
PfamPF02224. Cytidylate_kin. 1 hit.
PF02569. Pantoate_ligase. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00017. cmk. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANCY_PROM0
AccessionPrimary (citable) accession number: A3PF80
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 3, 2007
Last modified: June 11, 2014
This is version 52 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