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Protein

Phosphopantetheine adenylyltransferase

Gene

coaD

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 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 annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

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. Pantothenate kinase (coaA), Type III pantothenate kinase (coaX)
  2. Probable coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
  3. Probable coenzyme A biosynthesis bifunctional protein CoaBC (coaBC)
  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 annotation1
Binding sitei18ATPUniRule annotationCombined sources1 Publication1
Sitei18Transition state stabilizerUniRule annotation1
Binding sitei42SubstrateUniRule annotation1
Binding sitei74Substrate; via amide nitrogenUniRule annotation1
Binding sitei88SubstrateUniRule annotation1
Binding sitei99ATPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 11ATPUniRule annotationCombined sources1 Publication2
Nucleotide bindingi88 – 89ATPCombined sources1 Publication2
Nucleotide bindingi124 – 130ATPUniRule annotation1 Publication7

GO - Molecular functioni

GO - Biological processi

Keywordsi

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

Enzyme and pathway databases

BioCyciBSUB:BSU15020-MONOMER.
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:coaD1 PublicationUniRule annotation
Synonyms:ylbI
Ordered Locus Names:BSU15020
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001561691 – 161Phosphopantetheine adenylyltransferaseAdd BLAST161

Proteomic databases

PaxDbiO34797.
PRIDEiO34797.

Interactioni

Subunit structurei

Homohexamer.UniRule annotation

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100008306.

Structurei

Secondary structure

1161
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Helixi16 – 28Combined sources13
Beta strandi29 – 36Combined sources8
Helixi48 – 59Combined sources12
Beta strandi65 – 69Combined sources5
Helixi74 – 80Combined sources7
Beta strandi84 – 90Combined sources7
Helixi93 – 95Combined sources3
Helixi96 – 109Combined sources14
Beta strandi113 – 119Combined sources7
Turni123 – 126Combined sources4
Helixi129 – 137Combined sources9
Turni143 – 145Combined sources3
Helixi148 – 159Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1O6BX-ray2.20A2-161[»]
ProteinModelPortaliO34797.
SMRiO34797.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO34797.

Family & Domainsi

Sequence similaritiesi

Belongs to the bacterial CoaD family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108ZEF. Bacteria.
COG0669. LUCA.
HOGENOMiHOG000006518.
InParanoidiO34797.
KOiK00954.
OMAiEFQMALM.
PhylomeDBiO34797.

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.

O34797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASIAVCPGS FDPVTYGHLD IIKRGAHIFE QVYVCVLNNS SKKPLFSVEE
60 70 80 90 100
RCELLREVTK DIPNITVETS QGLLIDYAKR KNAKAILRGL RAVSDFEYEM
110 120 130 140 150
QGTSVNRVLD ESIETFFMMT NNQYSFLSSS IVKEVARYNG SVSEFVPPEV
160
ELALQQKFRQ G
Length:161
Mass (Da):18,179
Last modified:January 1, 1998 - v1
Checksum:iF4C23D80E359EA8F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z98682 Genomic DNA. Translation: CAB11355.1.
AL009126 Genomic DNA. Translation: CAB13375.1.
PIRiF69874.
RefSeqiNP_389385.1. NC_000964.3.
WP_003245283.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13375; CAB13375; BSU15020.
GeneIDi936889.
KEGGibsu:BSU15020.
PATRICifig|224308.179.peg.1637.

Similar proteinsi

Entry informationi

Entry nameiCOAD_BACSU
AccessioniPrimary (citable) accession number: O34797
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: October 25, 2017
This is version 135 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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