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Reviewed, UniProtKB/Swiss-Prot Q46526 (COAE_DICNO)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dephospho-CoA kinase
    EC=2.7.1.24
Alternative name(s):
    Dephosphocoenzyme A kinase
Gene names
Name: coaE
OrganismDichelobacter nodosus (Bacteroides nodosus)
Taxonomic identifier870 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCardiobacterialesCardiobacteriaceaeDichelobacter

Protein attributes

Sequence length197 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A By similarity.

Catalytic activity

ATP + 3'-dephospho-CoA = ADP + CoA. HAMAP MF_00376

Pathway

Cofactor biosynthesis; coenzyme A biosynthesis; coenzyme A from pantothenate: step 5/5. HAMAP MF_00376

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the coaE family.

Contains 1 DPCK (dephospho-CoA kinase) domain.

Ontologies

Keywords
   Biological processCoenzyme A biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Gene Ontology (GO)
   Biological processcoenzyme A biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

dephospho-CoA kinase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 197197Dephospho-CoA kinase HAMAP MF_00376
PRO_0000172905

Regions

Domain2 – 197196DPCK
Nucleotide binding7 – 148ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q46526-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 24FB4AC7A933BEE0

FASTA19722,161
        10         20         30         40         50         60 
MIVGLTGGIA SGKTLCCNWF AAQGCYIIDA DLIAKELVTV GGVVWLQLRA HFGETIFYAD 

        70         80         90        100        110        120 
GNLNRALLRE KMFHNQEIKE KVNQIFHPAV RAEIEKRIHL YPHAFTLLDV PLLFETQLHK 

       130        140        150        160        170        180 
ICHMVIVVDI PVSLQIARGV CRDGVNSAQM QRIIASQISR EKRLSLANFI IDNSNSIAQT 

       190 
YQQCQQIYQQ ILSLNAA 

« Hide

References

[1]"Identification of fimbrial assembly genes from Dichelobacter nodosus: evidence that fimP encodes the type-IV prepilin peptidase."
Johnston J.L., Billington S.J., Haring V., Rood J.I.
Gene 161:21-26(1995) [PubMed: 7642131] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: A198.

Cross-references

Sequence databases

U17138 Genomic DNA. Translation: AAB65808.1.

3D structure databases

HSSPHSSP built from PDB template 1N3B based on UniProtKB P36679.
ModBaseSearch...

Enzyme and pathway databases

BRENDA2.7.1.24. 289778.

Family and domain databases

HAMAPMF_00376.
[Tree]
InterProIPR001977. Depp_CoAkinase.
[Graphical view]
PANTHERPTHR10695. Depp_CoAkinase. 1 hit.
PfamPF01121. CoaE. 1 hit.
[Graphical view]
ProDomPD003329. Depp_CoAkinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00152. Depp_CoAkinase. 1 hit.
PROSITEPS51219. DPCK. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCOAE_DICNO
AccessionPrimary (citable) accession number: Q46526
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents