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O34797 (COAD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:ylbI
Ordered Locus Names:BSU15020
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length161 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate By similarity. 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 By similarity. HAMAP MF_00151

Subcellular location

Cytoplasm By similarity HAMAP MF_00151.

Sequence similarities

Belongs to the bacterial CoaD family.

Ontologies

Keywords
   Biological processCoenzyme A biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionNucleotidyltransferase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcoenzyme A biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

pantetheine-phosphate adenylyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161Phosphopantetheine adenylyltransferase HAMAP MF_00151
PRO_0000156169

Secondary structure

1 ........................... 161
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34797 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: F4C23D80E359EA8F

FASTA16118,179
        10         20         30         40         50         60 
MASIAVCPGS FDPVTYGHLD IIKRGAHIFE QVYVCVLNNS SKKPLFSVEE RCELLREVTK 

        70         80         90        100        110        120 
DIPNITVETS QGLLIDYAKR KNAKAILRGL RAVSDFEYEM QGTSVNRVLD ESIETFFMMT 

       130        140        150        160 
NNQYSFLSSS IVKEVARYNG SVSEFVPPEV ELALQQKFRQ G

« Hide

References

« Hide 'large scale' references
[1]"Bacillus subtilis chromosomal region downstream nprE."
Bertero M., Presecan E., Glaser P., Richou A., Danchin A.
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z98682 Genomic DNA. Translation: CAB11355.1.
AL009126 Genomic DNA. Translation: CAB13375.1.
PIRF69874.
RefSeqNP_389385.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1O6BX-ray2.20A2-161[»]
ProteinModelPortalO34797.
SMRO34797. Positions 2-161.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001125; EBBACP00000001125; EBBACG00000001123.
GeneID936889.
GenomeReviewsGene locus BSU15020 in contig AL009126_GR.
KEGGbsu:BSU15020.
NMPDRfig|224308.1.peg.1504.
PATRIC18974805. VBIBacSub10457_1594.

Organism-specific databases

GenoListBSU15020. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000002538.
HOGENOMHBG288308.
OMAAMSDFEY.
PhylomeDBO34797.
ProtClustDBPRK00168.

Enzyme and pathway databases

BioCycBSUB:BSU15020-MONOMER.

Family and domain databases

HAMAPMF_00151. PPAT_bact.
[Tree]
InterProIPR004821. Cyt_trans-rel.
IPR004820. Cytidylyltransf.
IPR001980. LPS_biosynth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK00954.
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
PRINTSPR01020. LPSBIOSNTHSS.
TIGRFAMsTIGR01510. CoaD_prev_kdtB. 1 hit.
TIGR00125. Cyt_tran_rel. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCOAD_BACSU
AccessionPrimary (citable) accession number: O34797
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents