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A8G795 (PANCY_PROM2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. 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:P9215_18631
OrganismProchlorococcus marinus (strain MIT 9215) [Complete proteome] [HAMAP]
Taxonomic identifier93060 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length510 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 – 510510Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_01349
PRO_0000333296

Regions

Nucleotide binding29 – 368ATP By similarity
Nucleotide binding150 – 1534ATP By similarity
Nucleotide binding187 – 1904ATP By similarity
Region1 – 276276Pantoate--beta-alanine ligase HAMAP-Rule MF_01349
Region277 – 510234Cytidylate kinase HAMAP-Rule MF_01349

Sites

Active site361Proton donor By similarity
Binding site611Beta-alanine By similarity
Binding site611Pantoate By similarity
Binding site1561Pantoate By similarity

Sequences

Sequence LengthMass (Da)Tools
A8G795 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: BC3128378F890BF4

FASTA51058,304
        10         20         30         40         50         60 
MKKVIIRKTE EIENWKRNIN NEINFIPTMG NLHNGHIKLI STAKNDNSNV NLVSIFINPL 

        70         80         90        100        110        120 
QFDNKLDLEN YPKTIDNDIK ISFSNGADAI FIPSNEDIYP PNNKNIKFLK APIELSSALC 

       130        140        150        160        170        180 
GLNRIGHFDG VCTVVYRLLN LIKPKNLYLG EKDWQQLLIL KNLVLKEKLN VAIKSIPTQR 

       190        200        210        220        230        240 
DFDGIPLSSR NVHLSKNERK LIRFFSSELL EAKKNFQQEK NINLNEIIKK LSAKKISIEY 

       250        260        270        280        290        300 
LEHLHPHTLQ KARLEDNISL LAGAIRCGET RLIDHVFLMK RRPIIAIDGP AGSGKSTVTK 

       310        320        330        340        350        360 
LIAKKLKLLY LDTGAMYRAL SWLLLKENID YKKEKKLLNI FKDISIVFKS NTNSHQDVYV 

       370        380        390        400        410        420 
NNCCVTEEIR SQKISSIVSK ISSIKEVRKF LVEEQRKIGE SGGLVAEGRD IGTTVFPNAE 

       430        440        450        460        470        480 
LKIFLTASID ERAKRRKSDK QSKDSQEIDL DTLKELIEKR DFEDSNREIS PLIKANDAIE 

       490        500        510 
IISDGYTINE VVDKIIDLYN DKIPKETEIK 

« 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: MIT 9215.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000825 Genomic DNA. Translation: ABV51476.1.
RefSeqYP_001485062.1. NC_009840.1.

3D structure databases

ProteinModelPortalA8G795.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93060.P9215_18631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABV51476; ABV51476; P9215_18631.
GeneID5615083.
KEGGpmh:P9215_18631.
PATRIC22993328. VBIProMar119824_1919.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycPMAR93060:GI08-1924-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_PROM2
AccessionPrimary (citable) accession number: A8G795
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 43 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