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Q3AUV1 (PANCY_SYNS9) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. 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:Syncc9902_1914
OrganismSynechococcus sp. (strain CC9902) [Complete proteome] [HAMAP]
Taxonomic identifier316279 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length483 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 – 483483Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_00158
PRO_0000239800

Regions

Nucleotide binding259 – 2679ATP By similarity
Region1 – 246246Pantoate--beta-alanine ligase HAMAP-Rule MF_00158
Region247 – 483237Cytidylate kinase HAMAP-Rule MF_00158

Sequences

Sequence LengthMass (Da)Tools
Q3AUV1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 32B97AA32D8CBC79

FASTA48352,124
        10         20         30         40         50         60 
MPTMGALHAG HGTVIRAASA MGPVLVSVFV NPLQFGPDED LARYPRSLES DLVVAERWGA 

        70         80         90        100        110        120 
AALWAPSVEQ IYPQGGERHP STIQVPPGLQ KHLCGAARPG HFDGVVTVVA RLLDLVRPRQ 

       130        140        150        160        170        180 
LWLGEKDWQQ LVILRWLVAH LARPVIVQGV ATVREADGLA LSSRNQYLSP DQRRMAAALP 

       190        200        210        220        230        240 
EALHAARGDG SDPIPALRGS LSDAGFEVEY VQRVDPCTLQ PCGDETAISL LAAAVRCGST 

       250        260        270        280        290        300 
RLIDHAFLMT RQPLVAIDGP AGAGKSTVTR AFAERLGLVY LDTGAMYRSV TWLVLERGVN 

       310        320        330        340        350        360 
PSDGVAIEPL LKDLDVQLQS LPGGVQQVLV NGEDVSSAIR SPDVTASVSA VAAHRCVRQA 

       370        380        390        400        410        420 
LTVQQKSMGS KGGLVAEGRD IGTAVFPHAD LKVFLTATVT ERARRRALDL EQRGFAVPER 

       430        440        450        460        470        480 
AELEAQIAER DRLDSTREEA PLMQADDAIE LVTDGMDIDA VIEALVRLFR ERVAEEAWPT 


PQR 

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9902."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9902.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000097 Genomic DNA. Translation: ABB26871.1.
RefSeqYP_377915.1. NC_007513.1.

3D structure databases

ProteinModelPortalQ3AUV1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316279.Syncc9902_1914.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB26871; ABB26871; Syncc9902_1914.
GeneID3742757.
KEGGsye:Syncc9902_1914.
PATRIC23801367. VBISynSp76179_2122.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSP316279:GJCI-1942-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:SF1. PTHR21299:SF1. 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_SYNS9
AccessionPrimary (citable) accession number: Q3AUV1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: November 22, 2005
Last modified: April 16, 2014
This is version 55 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