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Protein

Phosphopantetheine adenylyltransferase

Gene

coaD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA.UniRule annotation

Pathwayi

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • pantetheine-phosphate adenylyltransferase activity Source: EcoCyc

GO - Biological processi

  • coenzyme A biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Coenzyme A biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:PANTEPADENYLYLTRAN-MONOMER.
ECOL316407:JW3609-MONOMER.
MetaCyc:PANTEPADENYLYLTRAN-MONOMER.
BRENDAi2.7.7.3. 2026.
SABIO-RKP0A6I6.
UniPathwayiUPA00241; UER00355.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphopantetheine adenylyltransferaseUniRule annotation (EC:2.7.7.3UniRule annotation)
Alternative name(s):
Dephospho-CoA pyrophosphorylaseUniRule annotation
Pantetheine-phosphate adenylyltransferaseUniRule annotation
Short name:
PPATUniRule annotation
Gene namesi
Name:coaDUniRule annotation
Synonyms:kdtB, yicA
Ordered Locus Names:b3634, JW3609
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11190. coaD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 159159Phosphopantetheine adenylyltransferasePRO_0000156204Add
BLAST

Expressioni

Gene expression databases

GenevestigatoriP0A6I6.

Interactioni

Subunit structurei

Homohexamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
rplDP607231EBI-553173,EBI-545597

Protein-protein interaction databases

DIPiDIP-35966N.
IntActiP0A6I6. 10 interactions.
STRINGi511145.b3634.

Structurei

Secondary structure

1
159
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 96Combined sources
Helixi16 – 2611Combined sources
Beta strandi29 – 3810Combined sources
Helixi48 – 5811Combined sources
Turni59 – 613Combined sources
Beta strandi65 – 706Combined sources
Helixi74 – 807Combined sources
Beta strandi85 – 895Combined sources
Helixi96 – 10914Combined sources
Beta strandi113 – 1186Combined sources
Helixi122 – 1243Combined sources
Helixi129 – 1379Combined sources
Helixi143 – 1453Combined sources
Helixi148 – 15811Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B6TX-ray1.80A/B1-159[»]
1GN8X-ray1.83A/B1-159[»]
1H1TX-ray1.78A/B1-159[»]
1QJCX-ray1.64A/B2-159[»]
ProteinModelPortaliP0A6I6.
SMRiP0A6I6. Positions 3-159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6I6.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial CoaD family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0669.
HOGENOMiHOG000006518.
InParanoidiP0A6I6.
KOiK00954.
OMAiRAMSDFE.
OrthoDBiEOG6MH5J7.
PhylomeDBiP0A6I6.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00151. PPAT_bact.
InterProiIPR004821. Cyt_trans-like.
IPR001980. LPS_biosynth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
PRINTSiPR01020. LPSBIOSNTHSS.
TIGRFAMsiTIGR01510. coaD_prev_kdtB. 1 hit.
TIGR00125. cyt_tran_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6I6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKRAIYPGT FDPITNGHID IVTRATQMFD HVILAIAASP SKKPMFTLEE
60 70 80 90 100
RVALAQQATA HLGNVEVVGF SDLMANFARN QHATVLIRGL RAVADFEYEM
110 120 130 140 150
QLAHMNRHLM PELESVFLMP SKEWSFISSS LVKEVARHQG DVTHFLPENV

HQALMAKLA
Length:159
Mass (Da):17,837
Last modified:March 29, 2005 - v1
Checksum:iC4D7B8715A061B91
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJU0468.
RefSeqiNP_418091.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76658; AAC76658; b3634.
BAE77658; BAE77658; BAE77658.
GeneIDi947386.
KEGGiecj:Y75_p3540.
eco:b3634.
PATRICi32122755. VBIEscCol129921_3754.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJU0468.
RefSeqiNP_418091.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B6TX-ray1.80A/B1-159[»]
1GN8X-ray1.83A/B1-159[»]
1H1TX-ray1.78A/B1-159[»]
1QJCX-ray1.64A/B2-159[»]
ProteinModelPortaliP0A6I6.
SMRiP0A6I6. Positions 3-159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35966N.
IntActiP0A6I6. 10 interactions.
STRINGi511145.b3634.

Chemistry

BindingDBiP0A6I6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76658; AAC76658; b3634.
BAE77658; BAE77658; BAE77658.
GeneIDi947386.
KEGGiecj:Y75_p3540.
eco:b3634.
PATRICi32122755. VBIEscCol129921_3754.

Organism-specific databases

EchoBASEiEB1176.
EcoGeneiEG11190. coaD.

Phylogenomic databases

eggNOGiCOG0669.
HOGENOMiHOG000006518.
InParanoidiP0A6I6.
KOiK00954.
OMAiRAMSDFE.
OrthoDBiEOG6MH5J7.
PhylomeDBiP0A6I6.

Enzyme and pathway databases

UniPathwayiUPA00241; UER00355.
BioCyciEcoCyc:PANTEPADENYLYLTRAN-MONOMER.
ECOL316407:JW3609-MONOMER.
MetaCyc:PANTEPADENYLYLTRAN-MONOMER.
BRENDAi2.7.7.3. 2026.
SABIO-RKP0A6I6.

Miscellaneous databases

EvolutionaryTraceiP0A6I6.
PROiP0A6I6.

Gene expression databases

GenevestigatoriP0A6I6.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00151. PPAT_bact.
InterProiIPR004821. Cyt_trans-like.
IPR001980. LPS_biosynth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
PRINTSiPR01020. LPSBIOSNTHSS.
TIGRFAMsiTIGR01510. coaD_prev_kdtB. 1 hit.
TIGR00125. cyt_tran_rel. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiCOAD_ECOLI
AccessioniPrimary (citable) accession number: P0A6I6
Secondary accession number(s): P23875, Q2M7U8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: May 27, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.