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Q3AMJ0 (PANCY_SYNSC) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 59. 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. Pantoate--beta-alanine ligase
    EC=6.3.2.1
    Alternative name(s):
    Pantoate-activating enzyme
    Pantothenate synthetase
  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:Syncc9605_0416
OrganismSynechococcus sp. (strain CC9605) [Complete proteome] [HAMAP]
Taxonomic identifier110662 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length480 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + (R)-pantoate + beta-alanine = AMP + diphosphate + (R)-pantothenate. HAMAP-Rule MF_00158

ATP + (d)CMP = ADP + (d)CDP. 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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00158.

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 – 480480Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_00158
PRO_0000239801

Regions

Nucleotide binding256 – 2649ATP By similarity
Region1 – 243243Pantoate--beta-alanine ligase HAMAP-Rule MF_00158
Region244 – 480237Cytidylate kinase HAMAP-Rule MF_00158

Sequences

Sequence LengthMass (Da)Tools
Q3AMJ0 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 788E57AE99718559

FASTA48051,297
        10         20         30         40         50         60 
MPTMGGLHQG HGELIRRASE QGPVLVSVFV NPLQFGPAED FDRYPRTLEA DRGLAECCGA 

        70         80         90        100        110        120 
HALWAPSVDA IYPSGLPSAV SRSAPAGLQT HLCGASRPGH FDGVVTVVAR LLQLVEPSCL 

       130        140        150        160        170        180 
WLGEKDWQQL VILRRLVVDL DLGVVVKGVP TVRESDGLAL SSRNQYLFPA DRARAAALPA 

       190        200        210        220        230        240 
ALRHADPSDP ESSVRQSLAK AGLEVEYVER VDPRTLQPCG PETAISLLAA AVRCGTTRLI 

       250        260        270        280        290        300 
DHVFLMTRQP LVAIDGPAGA GKSTVTRAFA ERMGLVYLDT GAMYRSVTWL VQQNGVDHQD 

       310        320        330        340        350        360 
AVSIAPLLND LDLQLKSLPG GGQQVLVNGQ DVSDAIRSPE VTASVSAVAA HRCVRQALTA 

       370        380        390        400        410        420 
QQKAMGAKGG LVAEGRDIGT AVFPDADLKV FLTATVGERA RRRALDLEQR GFPVPERSEL 

       430        440        450        460        470        480 
EAQIAERDHL DSTREEAPLV QADDALELVT DGMSIEAVID ALVGQFRSRV GEEAWPTPAG 

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9605."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Martinez M., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9605.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000110 Genomic DNA. Translation: ABB34192.1.
RefSeqYP_380747.1. NC_007516.1.

3D structure databases

ProteinModelPortalQ3AMJ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING110662.Syncc9605_0416.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB34192; ABB34192; Syncc9605_0416.
GeneID3736513.
KEGGsyd:Syncc9605_0416.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0283.
HOGENOMHOG000233355.
KOK13799.
OMALGEKDWQ.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycSSP110662:GJ7R-430-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.
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.
PfamPF02569. Pantoate_ligase. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00017. cmk. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANCY_SYNSC
AccessionPrimary (citable) accession number: Q3AMJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: November 22, 2005
Last modified: June 11, 2014
This is version 59 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