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B0C6S1 (PANCY_ACAM1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 44. 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:AM1_2620
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesAcaryochloris

Protein attributes

Sequence length525 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 – 525525Bifunctional pantoate ligase/cytidylate kinase HAMAP-Rule MF_01349
PRO_0000333294

Regions

Nucleotide binding44 – 518ATP By similarity
Nucleotide binding162 – 1654ATP By similarity
Nucleotide binding199 – 2024ATP By similarity
Region1 – 292292Pantoate--beta-alanine ligase HAMAP-Rule MF_01349
Region293 – 525233Cytidylate kinase HAMAP-Rule MF_01349

Sites

Active site511Proton donor By similarity
Binding site751Beta-alanine By similarity
Binding site751Pantoate By similarity
Binding site1681Pantoate By similarity
Binding site1911ATP; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
B0C6S1 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: EE2A7EA486E0C84A

FASTA52557,533
        10         20         30         40         50         60 
MDNVPIIRTV SGLRHFLRCF PGNLNTGASP SSTVIGQIGL VPTMGALHAG HLSLIQRARQ 

        70         80         90        100        110        120 
ENQCVIVSIF VNPLQFAAHE DLTEYPQTLN QDQALCQEQG VNTIFAPSTD TLLADAPLTQ 

       130        140        150        160        170        180 
VIPPASLTEY LCGPHRPDHF TGVATIVLKL LNIVQPTRAY FGQKDAQQLA IIQRLVQDFN 

       190        200        210        220        230        240 
LDVTIVPCKL IRDATGLALS SRNQYLNAQE AQQATILHHS LQAARHTFQG GSCDRNSVLA 

       250        260        270        280        290        300 
TVAQTLAKGP QVEVEYIDLV DPVTLQPLEQ ITTQGLVAIA ARVGSARLID NMLLDARLPI 

       310        320        330        340        350        360 
LAIDGPAGAG KSTVTRRCAQ AIGLQYLDTG AMYRAVAWLA LDQQVEVSDP FAIADLVEDC 

       370        380        390        400        410        420 
QIELKPHADP QQQPQVWVNH QEVTQAIRTP DVTALVSAVA AQPPVREALV KQQQRLGRQG 

       430        440        450        460        470        480 
GLIAEGRDIG TNVFPDAGLK IFLTASIEER ARRRQQDLKN QNLPPQTQSE LEDLIASRDQ 

       490        500        510        520 
QDSQREFAPL RKAYDAVEIN TDGMTIEQVI TRITTLYQER FPDRA 

« Hide

References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MBIC 11017.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000828 Genomic DNA. Translation: ABW27627.1.
RefSeqYP_001516941.1. NC_009925.1.

3D structure databases

ProteinModelPortalB0C6S1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING329726.AM1_2620.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW27627; ABW27627; AM1_2620.
GeneID5681432.
KEGGamr:AM1_2620.
PATRIC20619536. VBIAcaMar40141_2401.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0283.
HOGENOMHOG000233355.
KOK13799.
OMALGEKDWQ.
OrthoDBEOG6Z6FZ4.

Enzyme and pathway databases

BioCycAMAR329726:GCZJ-2609-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.
InterProIPR004821. Cyt_trans-like.
IPR003136. 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.
TIGR00125. cyt_tran_rel. 1 hit.
TIGR00018. panC. 1 hit.
ProtoNetSearch...

Entry information

Entry namePANCY_ACAM1
AccessionPrimary (citable) accession number: B0C6S1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: June 11, 2014
This is version 44 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