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Protein

Phosphopantetheine adenylyltransferase

Gene

coaD

Organism
Staphylococcus aureus (strain MW2)
Status
Reviewed-Annotation score: -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

Is inhibited by a series of cycloalkyl pyrimidines, which also show suppression of bacterial growth.1 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 II pantothenate kinase (coaW)
  2. Coenzyme A biosynthesis bifunctional protein CoaBC (MW1094)
  3. Coenzyme A biosynthesis bifunctional protein CoaBC (MW1094)
  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 sitei11SubstrateUniRule annotation1
Binding sitei19ATPUniRule annotationCombined sources1 Publication1
Binding sitei43SubstrateUniRule annotation1
Binding sitei75Substrate; via amide nitrogenUniRule annotation1
Binding sitei89SubstrateUniRule annotation1
Binding sitei100ATPUniRule annotationCombined sources1 Publication1
Binding sitei121ATPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 12ATPUniRule annotationCombined sources1 Publication2
Nucleotide bindingi90 – 92ATPUniRule annotationCombined sources1 Publication3
Nucleotide bindingi125 – 131ATPUniRule annotationCombined sources1 Publication7

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

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:coaD1 PublicationUniRule annotation
Ordered Locus Names:MW1007
OrganismiStaphylococcus aureus (strain MW2)
Taxonomic identifieri196620 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000000418 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Biotechnological usei

PPAT is a validated novel target for antibacterial therapy against Gram-positive bacteria.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001562761 – 160Phosphopantetheine adenylyltransferaseAdd BLAST160

Interactioni

Subunit structurei

Homohexamer.UniRule annotation1 Publication

Structurei

Secondary structure

1160
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Helixi17 – 26Combined sources10
Helixi27 – 29Combined sources3
Beta strandi30 – 37Combined sources8
Helixi49 – 59Combined sources11
Turni60 – 62Combined sources3
Beta strandi66 – 70Combined sources5
Helixi75 – 82Combined sources8
Beta strandi86 – 91Combined sources6
Helixi94 – 110Combined sources17
Beta strandi115 – 120Combined sources6
Helixi123 – 125Combined sources3
Helixi130 – 138Combined sources9
Turni144 – 146Combined sources3
Helixi149 – 159Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4NAHX-ray2.38A/B/C/D/E/F1-160[»]
4NATX-ray1.72A/B/C1-160[»]
4NAUX-ray2.33A/B/C1-160[»]
ProteinModelPortaliP63820
SMRiP63820
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63820

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial CoaD family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000006518
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
PANTHERiPTHR21342:SF1 PTHR21342:SF1, 1 hit
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.

P63820-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEHTIAVIPG SFDPITYGHL DIIERSTDRF DEIHVCVLKN SKKEGTFSLE
60 70 80 90 100
ERMDLIEQSV KHLPNVKVHQ FSGLLVDYCE QVGAKTIIRG LRAVSDFEYE
110 120 130 140 150
LRLTSMNKKL NNEIETLYMM SSTNYSFISS SIVKEVAAYR ADISEFVPPY
160
VEKALKKKFK
Length:160
Mass (Da):18,371
Last modified:October 11, 2004 - v1
Checksum:i67B4E6F42DBC8D41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000033 Genomic DNA Translation: BAB94872.1
RefSeqiWP_000401377.1, NC_003923.1

Genome annotation databases

EnsemblBacteriaiBAB94872; BAB94872; BAB94872
KEGGisam:MW1007

Similar proteinsi

Entry informationi

Entry nameiCOAD_STAAW
AccessioniPrimary (citable) accession number: P63820
Secondary accession number(s): Q99UX9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: March 28, 2018
This is version 85 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

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