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Q7UZR6 (PANCY_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. 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:PMM1590
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length510 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 – 510510Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_00158
PRO_0000239792

Regions

Nucleotide binding289 – 2979ATP By similarity
Region1 – 276276Pantoate--beta-alanine ligase HAMAP-Rule MF_00158
Region277 – 510234Cytidylate kinase HAMAP-Rule MF_00158

Sequences

Sequence LengthMass (Da)Tools
Q7UZR6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 315DC94E014CBDF8

FASTA51058,295
        10         20         30         40         50         60 
MNKIIIRKTE DLKEWRRNLK CDINFIPTMG NLHDGHQKLI STAQSSNCNT NLLSIFVNPL 

        70         80         90        100        110        120 
QFDSKEDLKS YPKTVDKDIE IAFSNGADAI FIPNVTDIYP KKNKSISYLK ASKELSSALC 

       130        140        150        160        170        180 
GLTRVGHFDG VCTVVYRLLK LIQPKNLFLG EKDWQQLLII KNLIEEKKFN IKIIPVPTQR 

       190        200        210        220        230        240 
DSDGVPFSSR NKHLSKSERK SLKLFSNELE NAKIIFKKDK RIDLKQLTNK LKSKNISIEY 

       250        260        270        280        290        300 
LEHLHPYSLK KVQSNDNISI LAGAIKCGKT RLIDHVFLMK RKPIIAIDGP AGSGKSTITK 

       310        320        330        340        350        360 
LIAKELNLLY LDTGAMYRAI SWLFKKEKID YAKESELKKI LNNISIIFKS NSISQQDVFI 

       370        380        390        400        410        420 
NNFCVTEEIR SQEISSIVSK ISSIKKVREF LVYEQRKIGQ SGGLVAEGRD IGTTVFPNAE 

       430        440        450        460        470        480 
LKIFLTASID ERAKRRKSEL DLRGTEEIDF NQLRELIRKR DFEDSTRKIS PLKKANDAIE 

       490        500        510 
LLTDGYSINE VVEKIVNIYN LNIPKEIQLE 

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX548174 Genomic DNA. Translation: CAE20049.1.
RefSeqNP_893707.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7UZR6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59919.PMM1590.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE20049; CAE20049; PMM1590.
GeneID1726235.
KEGGpmm:PMM1590.
PATRIC23034364. VBIProMar68066_1831.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0283.
HOGENOMHOG000233355.
KOK13799.
OMALGEKDWQ.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycPMAR59919:GJMQ-1634-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_PROMP
AccessionPrimary (citable) accession number: Q7UZR6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 69 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