Phosphopantetheine adenylyltransferase - Escherichia coli (strain K12)

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P0A6I6 (COAD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	159 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Coenzyme A biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	coenzyme A biosynthetic process Inferred from direct assay PubMed 17873050. Source: EcoCyc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pantetheine-phosphate adenylyltransferase activity Inferred from direct assay PubMed 17873050. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rplD	P60723	1	EBI-553173,EBI-545597

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 159

159

Phosphopantetheine adenylyltransferase HAMAP-Rule MF_00151

PRO_0000156204

Secondary structure

159

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6I6 [UniParc].

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

159

17,837

        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' referencesShow '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 277:1453-1474(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.

PIR

JU0468.

RefSeq

NP_418091.1. NC_000913.2.
YP_491799.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B6T	X-ray	1.80	A/B	1-159	[»]
1GN8	X-ray	1.83	A/B	1-159	[»]
1H1T	X-ray	1.78	A/B	1-159	[»]
1QJC	X-ray	1.64	A/B	2-159	[»]

ProteinModelPortal

P0A6I6.

SMR

P0A6I6. Positions 3-159.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35966N.

IntAct

P0A6I6. 10 interactions.

STRING

511145.b3634.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76658; AAC76658; b3634.
BAE77658; BAE77658; BAE77658.

GeneID

12934385.
947386.

KEGG

ecj:Y75_p3540.
eco:b3634.

PATRIC

32122755. VBIEscCol129921_3754.

Organism-specific databases

EchoBASE

EB1176.

EcoGene

EG11190. coaD.

Phylogenomic databases

eggNOG

COG0669.

HOGENOM

HOG000006518.

K00954.

OMA

AMSDFEY.

ProtClustDB

PRK00168.

Enzyme and pathway databases

BioCyc

EcoCyc:PANTEPADENYLYLTRAN-MONOMER.
ECOL316407:JW3609-MONOMER.
MetaCyc:PANTEPADENYLYLTRAN-MONOMER.

SABIO-RK

P0A6I6.

UniPathway

UPA00241; UER00355.

Gene expression databases

Genevestigator

P0A6I6.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

HAMAP

MF_00151. PPAT_bact.

InterPro

IPR004821. Cyt_trans-like.
IPR001980. LPS_biosynth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Pfam

PF01467. CTP_transf_2. 1 hit.
[Graphical view]

PRINTS

PR01020. LPSBIOSNTHSS.

TIGRFAMs

TIGR01510. coaD_prev_kdtB. 1 hit.
TIGR00125. cyt_tran_rel. 1 hit.

ProtoNet

Search...

Other

BindingDB

P0A6I6.

EvolutionaryTrace

P0A6I6.

Entry information

Entry name

COAD_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents