Reviewed, UniProtKB/Swiss-Prot P0A6I6 (COAD_ECOLI)

Names and origin

Protein names

Recommended name:
    Phosphopantetheine adenylyltransferase
    EC=2.7.7.3
Alternative name(s):
    Pantetheine-phosphate adenylyltransferase
      Short name=PPAT
    Dephospho-CoA pyrophosphorylase

Gene names

Name:	coaD
Synonyms:	kdtB, yicA
Ordered Locus Names:	b3634, JW3609

Organism

Escherichia coli (strain K12) [Complete 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 MF_00151
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. HAMAP MF_00151
Subcellular location	Cytoplasm HAMAP 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
Gene Ontology (GO)
Biological process	coenzyme A biosynthetic process Inferred from direct assay. Source: UniProtKB
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. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
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 MF_00151

PRO_0000156204

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

159

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

16 – 28

13

Beta strand

29 – 39

11

Helix

48 – 58

11

Turn

59 – 61

3

Beta strand

65 – 70

6

Helix

74 – 80

7

Beta strand

85 – 89

5

Helix

96 – 109

14

Beta strand

113 – 118

6

Helix

122 – 124

3

Helix

129 – 137

9

Helix

143 – 145

3

Helix

148 – 158

11

Sequences

	Sequence		Length	Mass (Da)
	P0A6I6-1 [UniParc]. Last modified March 29, 2005. Version 1. Checksum: C4D7B8715A061B91	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

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: 2033061] [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: 8041620] [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: 9278503] [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: 16738553] [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: 10480925] [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: 1577693] [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: 10205156] [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: 11812124] [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

AP_004157.1.
NP_418091.1.

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A6I6. 10 interactions.

STRING

P0A6I6.

Genome annotation databases

GeneID

947386.

GenomeReviews

Gene locus JW3609 in contig AP009048_GR.
Gene locus b3634 in contig U00096_GR.

KEGG

ecj:JW3609.
eco:b3634.

Organism-specific databases

EchoBASE

EB1176.

EcoGene

EG11190. coaD.

CMR

Search...

Phylogenomic databases

eggNOG

COG0669.

HOGENOM

HBG288308.

OMA

VRQIAAM.

Enzyme and pathway databases

BioCyc

EcoCyc:PANTEPADENYLYLTRAN-MONOMER.
ECOL168927:B3634-MONOMER.
MetaCyc:PANTEPADENYLYLTRAN-MONOMER.

Gene expression databases

Genevestigator

P0A6I6.

Family and domain databases

HAMAP

MF_00151. PPAT_bact.
[Tree]

InterPro

IPR004821. Cyt_trans_rel.
IPR004820. Cytidylyltransf.
IPR001980. LPS_biosynth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Gene3D

G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.

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...

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:	February 9, 2010
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)