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Reviewed, UniProtKB/Swiss-Prot A5EJR7 (COAD_BRASB)

Last modified November 3, 2009. Version 17. 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:
    Phosphopantetheine adenylyltransferase
    EC=2.7.7.3
Alternative name(s):
    Pantetheine-phosphate adenylyltransferase
      Short name=PPAT
    Dephospho-CoA pyrophosphorylase
Gene names
Name: coaD
Ordered Locus Names: BBta_4369
OrganismBradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182) [Complete proteome] [HAMAP]
Taxonomic identifier288000 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate By similarity.

Catalytic activity

ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA. HAMAP MF_00151

Pathway

Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5. HAMAP MF_00151

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the bacterial coaD family.

Ontologies

Keywords
   Biological processCoenzyme A biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionNucleotidyltransferase
Transferase
   Technical termComplete proteome
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: UniProtKB-KW

pantetheine-phosphate adenylyltransferase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Phosphopantetheine adenylyltransferase HAMAP MF_00151
PRO_1000011098

Sequences

Sequence LengthMass (Da)Tools
A5EJR7-1 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 51C6560025A46E48

FASTA16417,417
        10         20         30         40         50         60 
MQRIALYPGS FDPVTNGHLD VVRQAVHLCD RLIVAVGVHH GKKPLFSTEE RLAMVHEVLE 

        70         80         90        100        110        120 
PVAAAAGCGF EASTYDDLTV TAAQKAGAIM MIRGLRDGTD FDYEMQLAGM NQTMVPGIQT 

       130        140        150        160 
VFVPASVAVR PIAATLVRQI AAMGGDVSHF VPAAVAASLK AKFN 

« Hide

Cross-references

Sequence databases

CP000494 Genomic DNA. Translation: ABQ36411.1.
RefSeqYP_001240317.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA5EJR7.

Genome annotation databases

GeneID5152558.
GenomeReviewsGene locus BBta_4369 in contig CP000494_GR.
KEGGbbt:BBta_4369.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAAMSDFEY.

Family and domain databases

HAMAPMF_00151.
[Tree]
InterProIPR004821. Cyt_trans_rel.
IPR004820. Cytidylyltransf.
IPR001980. LPS_biosynth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
PRINTSPR01020. LPSBIOSNTHSS.
TIGRFAMsTIGR01510. coaD_prev_kdtB. 1 hit.
TIGR00125. cyt_tran_rel. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCOAD_BRASB
AccessionPrimary (citable) accession number: A5EJR7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 12, 2007
Last modified: November 3, 2009
This is version 17 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