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Q110U9 (PANCY_TRIEI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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:Tery_2799
OrganismTrichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP]
Taxonomic identifier203124 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesTrichodesmium

Protein attributes

Sequence length528 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 – 528528Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_01349
PRO_0000333303

Regions

Nucleotide binding34 – 418ATP By similarity
Nucleotide binding160 – 1634ATP By similarity
Nucleotide binding197 – 2004ATP By similarity
Region1 – 293293Pantoate--beta-alanine ligase HAMAP-Rule MF_01349
Region294 – 528235Cytidylate kinase HAMAP-Rule MF_01349

Sites

Active site411Proton donor By similarity
Binding site651Beta-alanine By similarity
Binding site651Pantoate By similarity
Binding site1661Pantoate By similarity
Binding site1891ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q110U9 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: EC536758F6078812

FASTA52858,427
        10         20         30         40         50         60 
MRLFTTIAGL NCYLNLLRNE QKKSPDTIGL VPTMGALHKG HLSLIKRARE ENTITVVSIF 

        70         80         90        100        110        120 
INPLQFAPRE DFKEYPRQLE IDKEFCEKEG VDVIFAPTPE TMGMKNALST DAQDSTTTVV 

       130        140        150        160        170        180 
SPSHMTSIMC GVSRPNFFQG VATIVTKLLN IVKPNNAYFG QKDAQQLAII KQLVKDLSLP 

       190        200        210        220        230        240 
VNIVYCPIIR EASGLAISSR NQYLTPEQKE QASMLYASLC YGRKIFLENQ DTPNILETVE 

       250        260        270        280        290        300 
NAVKEKLASQ PVLKLEYLEI VDPETLKPLE NIQNIGLLAI AAYIGSCRLI DNILLRNRKP 

       310        320        330        340        350        360 
IIAIDGPAGA GKSTVTKLVG QSLGLLYLDT GAMYRAVTWM VLQSGVPVTD QAQVAELVSQ 

       370        380        390        400        410        420 
CQISFNSPEN NHVVINGQDV TVAIRSREVT NNVSIVAAQP TVRYFMVKQQ QQFGAKGGIV 

       430        440        450        460        470        480 
AEGRDIGSHV FPNAELKIFL TASLKERSRR RLVELKQKGQ TNISLEEVEK EIICRDQKDT 

       490        500        510        520 
NRKISPLRKS SDAVEISTDG LSIGEVTQKI VDIFKTTCYG KSSVNNII 

« Hide

References

[1]"Complete sequence of Trichodesmium erythraeum IMS101."
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., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IMS101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000393 Genomic DNA. Translation: ABG51975.1.
RefSeqYP_722448.1. NC_008312.1.

3D structure databases

ProteinModelPortalQ110U9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203124.Tery_2799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG51975; ABG51975; Tery_2799.
GeneID4245333.
KEGGter:Tery_2799.
PATRIC23990266. VBITriEry99848_3558.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0283.
HOGENOMHOG000233355.
KOK13799.
OMALGEKDWQ.
OrthoDBEOG6Z6FZ4.
ProtClustDBPRK13477.

Enzyme and pathway databases

BioCycTERY203124:GJDR-2825-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.
InterProIPR004821. Cyt_trans-like.
IPR003136. Cytidylate_kin.
IPR027417. P-loop_NTPase.
IPR003721. Pantoate_ligase.
IPR024894. Pantoate_ligase/cytidylate_kin.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21299:SF1. PTHR21299:SF1. 1 hit.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00017. cmk. 1 hit.
TIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANCY_TRIEI
AccessionPrimary (citable) accession number: Q110U9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: August 22, 2006
Last modified: April 16, 2014
This is version 56 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