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Q0ICW2 (PANCY_SYNS3) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. 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:sync_0483
OrganismSynechococcus sp. (strain CC9311) [Complete proteome] [HAMAP]
Taxonomic identifier64471 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length494 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 – 494494Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_01349
PRO_0000333300

Regions

Nucleotide binding7 – 148ATP By similarity
Nucleotide binding130 – 1334ATP By similarity
Nucleotide binding167 – 1704ATP By similarity
Region1 – 258258Pantoate--beta-alanine ligase HAMAP-Rule MF_01349
Region259 – 494236Cytidylate kinase HAMAP-Rule MF_01349

Sites

Active site141Proton donor By similarity
Binding site411Beta-alanine By similarity
Binding site411Pantoate By similarity
Binding site1361Pantoate By similarity
Binding site1591ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0ICW2 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: E7EDD078F93465E3

FASTA49453,594
        10         20         30         40         50         60 
MHFVPTMGGL HHGHASLISA ASCHKSGDVE TLVSVFVNPL QFGPNEDFAR YPRTFEADCE 

        70         80         90        100        110        120 
LAELSGASAI WCPDESQIYP GGSAESWRIQ APKSLQSRLC GSTRPGHFDG VVTVVCRLLA 

       130        140        150        160        170        180 
LAKPHQLFLG EKDWQQLTIL RRMVLDLGLA VRVRGVPTVR DGDGLASSSR NRYLNAQQRQ 

       190        200        210        220        230        240 
QGVLFAQVLS DARSACLHGG TALKPGEVKR RLEEVGLSVE YVDVVDPWFL QPSKSNQSSL 

       250        260        270        280        290        300 
TLLAAAVRCG STRLIDHAFL MTRSPLVAID GPAGAGKSTV TRAFAERLGL VYLDTGAMYR 

       310        320        330        340        350        360 
AVTWLVLEQG GDPGDSEAVD LVLNDLKVEL EPLQQGVQVV RVNGHEVTDA IRDPRVTASV 

       370        380        390        400        410        420 
SAVASHACVR AAMTAQQQRM GKAGGLVAEG RDIGTAVFPD AELKVFLTAT PKERARRRAL 

       430        440        450        460        470        480 
DLEARGHEVP ALPELEAQIV ERDRLDSTRE VAPLLQADDA IELISDGMSI DQVIDALEDL 

       490 
FRRRVGEEVW PTPV 

« Hide

References

[1]"Genome sequence of Synechococcus CC9311: insights into adaptation to a coastal environment."
Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H., Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S., Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R., Paulsen I.T.
Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9311.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000435 Genomic DNA. Translation: ABI45138.1.
RefSeqYP_729710.1. NC_008319.1.

3D structure databases

ProteinModelPortalQ0ICW2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING64471.sync_0483.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI45138; ABI45138; sync_0483.
GeneID4260685.
KEGGsyg:sync_0483.
PATRIC23791826. VBISynSp88089_0490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0283.
HOGENOMHOG000233355.
KOK13799.
OMALGEKDWQ.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycSSP64471:GIVP-483-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_SYNS3
AccessionPrimary (citable) accession number: Q0ICW2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 3, 2006
Last modified: June 11, 2014
This is version 54 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