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P0A6I6 (COAD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphopantetheine adenylyltransferase

EC=2.7.7.3
Alternative name(s):
Dephospho-CoA pyrophosphorylase
Pantetheine-phosphate adenylyltransferase
Short name=PPAT
Gene names
Name:coaD
Synonyms:kdtB, yicA
Ordered Locus Names:b3634, JW3609
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length159 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate. HAMAP-Rule MF_00151

Catalytic activity

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

Pathway

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

Subunit structure

Homohexamer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00151.

Sequence similarities

Belongs to the bacterial CoaD family.

Caution

Was originally thought to have an essential function in lipopolysaccharides biosynthesis.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rplDP607231EBI-553173,EBI-545597

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 159159Phosphopantetheine adenylyltransferase HAMAP-Rule MF_00151
PRO_0000156204

Secondary structure

............................ 159
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A6I6 [UniParc].

Last modified March 29, 2005. Version 1.
Checksum: C4D7B8715A061B91

FASTA15917,837
        10         20         30         40         50         60 
MQKRAIYPGT FDPITNGHID IVTRATQMFD HVILAIAASP SKKPMFTLEE RVALAQQATA 

        70         80         90        100        110        120 
HLGNVEVVGF SDLMANFARN QHATVLIRGL RAVADFEYEM QLAHMNRHLM PELESVFLMP 

       130        140        150 
SKEWSFISSS LVKEVARHQG DVTHFLPENV HQALMAKLA 

« Hide

References

« Hide 'large scale' references
[1]"A gene coding for 3-deoxy-D-manno-octulosonic-acid transferase in Escherichia coli. Identification, mapping, cloning, and sequencing."
Clementz T., Raetz C.R.H.
J. Biol. Chem. 266:9687-9696(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli."
Geerlof A., Lewendon A., Shaw W.V.
J. Biol. Chem. 274:27105-27111(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-10, CHARACTERIZATION.
[6]"Genetic analysis of the genes involved in synthesis of the lipopolysaccharide core in Escherichia coli K-12: three operons in the rfa locus."
Roncero C., Casadaban M.J.
J. Bacteriol. 174:3250-3260(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: GENETIC CHARACTERIZATION.
Strain: K12.
[7]"The crystal structure of a novel bacterial adenylyltransferase reveals half of sites reactivity."
Izard T., Geerlof A.
EMBO J. 18:2021-2030(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
[8]"The crystal structures of phosphopantetheine adenylyltransferase with bound substrates reveal the enzyme's catalytic mechanism."
Izard T.
J. Mol. Biol. 315:487-495(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60670 Genomic DNA. Translation: AAA24044.1.
M86305 Genomic DNA. Translation: AAA03746.1.
U00039 Genomic DNA. Translation: AAB18611.1.
U00096 Genomic DNA. Translation: AAC76658.1.
AP009048 Genomic DNA. Translation: BAE77658.1.
PIRJU0468.
RefSeqNP_418091.1. NC_000913.3.
YP_491799.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B6TX-ray1.80A/B1-159[»]
1GN8X-ray1.83A/B1-159[»]
1H1TX-ray1.78A/B1-159[»]
1QJCX-ray1.64A/B2-159[»]
ProteinModelPortalP0A6I6.
SMRP0A6I6. Positions 3-159.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-35966N.
IntActP0A6I6. 10 interactions.
STRING511145.b3634.

Chemistry

BindingDBP0A6I6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76658; AAC76658; b3634.
BAE77658; BAE77658; BAE77658.
GeneID12934385.
947386.
KEGGecj:Y75_p3540.
eco:b3634.
PATRIC32122755. VBIEscCol129921_3754.

Organism-specific databases

EchoBASEEB1176.
EcoGeneEG11190. coaD.

Phylogenomic databases

eggNOGCOG0669.
HOGENOMHOG000006518.
KOK00954.
OMAAMSDFEY.
OrthoDBEOG6MH5J7.
PhylomeDBP0A6I6.
ProtClustDBPRK00168.

Enzyme and pathway databases

BioCycEcoCyc:PANTEPADENYLYLTRAN-MONOMER.
ECOL316407:JW3609-MONOMER.
MetaCyc:PANTEPADENYLYLTRAN-MONOMER.
SABIO-RKP0A6I6.
UniPathwayUPA00241; UER00355.

Gene expression databases

GenevestigatorP0A6I6.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00151. PPAT_bact.
InterProIPR004821. Cyt_trans-like.
IPR001980. LPS_biosynth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
PRINTSPR01020. LPSBIOSNTHSS.
TIGRFAMsTIGR01510. coaD_prev_kdtB. 1 hit.
TIGR00125. cyt_tran_rel. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A6I6.
PROP0A6I6.

Entry information

Entry nameCOAD_ECOLI
AccessionPrimary (citable) accession number: P0A6I6
Secondary accession number(s): P23875, Q2M7U8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 86 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene