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Protein

Phosphopantetheine adenylyltransferase

Gene

coaD

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score: Annotation score: 5 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.UniRule annotation1 Publication

Catalytic activityi

ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA.UniRule annotation1 Publication

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Tightly binds to CoA, which is presumably a feedback inhibitor (PubMed:21527250). Potently inhibited by D-amethopterin, which simultaneously occupies the 4'-phosphopantetheine- and ATP-binding sites; following treatment with D-amethopterin, H.pylori exhibits morphological characteristics associated with cell death, showing that D-amethopterin displays antimicrobial activity (PubMed:24040220).1 Publication1 Publication

Pathwayi: coenzyme A biosynthesis

This protein is involved in step 4 of the subpathway that synthesizes CoA from (R)-pantothenate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Type III pantothenate kinase (coaX)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Phosphopantetheine adenylyltransferase (coaD)
  5. Dephospho-CoA kinase (coaE)
This subpathway is part of the pathway coenzyme A biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CoA from (R)-pantothenate, the pathway coenzyme A biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei10SubstrateUniRule annotationCombined sources1 Publication1
Binding sitei18ATPUniRule annotation1
Sitei18Transition state stabilizerUniRule annotation1
Binding sitei42SubstrateUniRule annotationCombined sources1 Publication1
Binding sitei74Substrate; via amide nitrogenUniRule annotationCombined sources1 Publication1
Binding sitei88SubstrateUniRule annotation1
Binding sitei99ATPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 11ATPUniRule annotation2
Nucleotide bindingi89 – 91ATPUniRule annotationCombined sources1 Publication3
Nucleotide bindingi124 – 130ATPUniRule annotation7

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processCoenzyme A biosynthesis
LigandATP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciHPY:HP1475-MONOMER.
BRENDAi2.7.7.3. 2604.
UniPathwayiUPA00241; UER00355.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphopantetheine adenylyltransferase1 PublicationUniRule annotation (EC:2.7.7.3UniRule annotation1 Publication)
Alternative name(s):
Dephospho-CoA pyrophosphorylaseUniRule annotation
Pantetheine-phosphate adenylyltransferaseUniRule annotation
Short name:
PPAT1 PublicationUniRule annotation
Gene namesi
Name:coaDUniRule annotation
Synonyms:kdtB
Ordered Locus Names:HP_1475
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
Proteomesi
  • UP000000429 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi4I → V: Forms a domain-swapped homotetramer; when associated with Y-76. 1 Publication1
Mutagenesisi76N → Y: Forms a domain-swapped homotetramer; when associated with V-4. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001562171 – 157Phosphopantetheine adenylyltransferaseAdd BLAST157

Proteomic databases

PaxDbiO26010.

Interactioni

Subunit structurei

Homohexamer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi85962.HP1475.

Structurei

Secondary structure

1157
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi16 – 26Combined sources11
Beta strandi29 – 37Combined sources9
Helixi40 – 42Combined sources3
Helixi48 – 59Combined sources12
Beta strandi65 – 70Combined sources6
Helixi74 – 80Combined sources7
Beta strandi85 – 89Combined sources5
Helixi96 – 108Combined sources13
Beta strandi114 – 118Combined sources5
Helixi122 – 125Combined sources4
Helixi129 – 137Combined sources9
Turni143 – 145Combined sources3
Turni148 – 150Combined sources3
Helixi151 – 154Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NV7X-ray1.75A1-157[»]
3OTWX-ray1.80A/B/C/D/E/F1-157[»]
ProteinModelPortaliO26010.
SMRiO26010.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO26010.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial CoaD family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108ZEF. Bacteria.
COG0669. LUCA.
KOiK00954.
OMAiEFQMALM.

Family and domain databases

CDDicd02163. PPAT. 1 hit.
Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00151. PPAT_bact. 1 hit.
InterProiView protein in InterPro
IPR004821. Cyt_trans-like.
IPR001980. PPAT.
IPR014729. Rossmann-like_a/b/a_fold.
PfamiView protein in Pfam
PF01467. CTP_transf_like. 1 hit.
PRINTSiPR01020. LPSBIOSNTHSS.
TIGRFAMsiTIGR01510. coaD_prev_kdtB. 1 hit.
TIGR00125. cyt_tran_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

O26010-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQKIGIYPGT FDPVTNGHID IIHRSSELFE KLIVAVAHSS AKNPMFSLDE
60 70 80 90 100
RLKMIQLATK SFKNVECVAF EGLLANLAKE YHCKVLVRGL RVVSDFEYEL
110 120 130 140 150
QMGYANKSLN HELETLYFMP TLQNAFISSS IVRSIIAHKG DASHLVPKEI

YPLISKA
Length:157
Mass (Da):17,668
Last modified:January 1, 1998 - v1
Checksum:i4250742EAB58E097
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD08514.1.
PIRiC64704.
RefSeqiNP_208266.1. NC_000915.1.
WP_001169234.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD08514; AAD08514; HP_1475.
GeneIDi899817.
KEGGiheo:C694_07635.
hpy:HP1475.
PATRICifig|85962.47.peg.1586.

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 one 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.

Entry informationi

Entry nameiCOAD_HELPY
AccessioniPrimary (citable) accession number: O26010
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 5, 2017
This is version 112 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  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