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Q46IM3 (PANCY_PROMT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. 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:PMN2A_1165
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length516 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 – 516516Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_00158
PRO_0000239793

Regions

Nucleotide binding292 – 3009ATP By similarity
Region1 – 279279Pantoate--beta-alanine ligase HAMAP-Rule MF_00158
Region280 – 516237Cytidylate kinase HAMAP-Rule MF_00158

Sequences

Sequence LengthMass (Da)Tools
Q46IM3 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 3980DA9C3BFB07FA

FASTA51658,289
        10         20         30         40         50         60 
MVRKIFQTNA ELKDWLSGQN SAIIFIPTMG GLHPGHQYLI QKAKEKKTNT NQIILVSIFV 

        70         80         90        100        110        120 
NPLQFSKGED FKKYPRNIKR DAELAFSAGA DAIWAPEYDE VFPGGADSHF KIEVPKTLHN 

       130        140        150        160        170        180 
QLCGAERKGH FDGVATVIIR LIKIIKPKKL ILGEKDWQQL IIIRKLFQEL SIPVKIESYS 

       190        200        210        220        230        240 
TQRDQSGFAY SSRNSYLSDS ERVNAQSLPN AIKEAKTEFD KGKVINLTKI ASIFKENNLK 

       250        260        270        280        290        300 
IEYLKIVDPF SLKETENINR LCLLAIAVKC GSTRLIDHTF LMHRKPIIAI DGPAGAGKST 

       310        320        330        340        350        360 
VTKAFAKKLG FIYLDTGAMY RAVTWLIISN SIDPNDQAEI KNILKDSKLE FKNSSFVEQK 

       370        380        390        400        410        420 
IFINNIDVTE KIRSPQVTSM VSEIAKQQFV REVLTRKQQV IGNNGGLVAE GRDIGTAVFP 

       430        440        450        460        470        480 
DADLKIFLTA SPTERAKRRA LDLHKRGYEF SSIEDLEKEI KERDKKDSER KIAPLKKAQD 

       490        500        510 
AIELVTDGMN IEDVLKELID IFRSKIPEEV WPTPNS 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NATL2A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ58655.1.
RefSeqYP_292358.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46IM3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59920.PMN2A_1165.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ58655; AAZ58655; PMN2A_1165.
GeneID3606556.
KEGGpmn:PMN2A_1165.
PATRIC23026215. VBIProMar14922_2031.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0283.
HOGENOMHOG000233355.
KOK13799.
OMALGEKDWQ.
OrthoDBEOG6Z6FZ4.
PhylomeDBQ46IM3.

Enzyme and pathway databases

BioCycPMAR59920:GI1O-2054-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_PROMT
AccessionPrimary (citable) accession number: Q46IM3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: September 13, 2005
Last modified: July 9, 2014
This is version 62 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