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P0A530 (COAD_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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:kdtB
Ordered Locus Names:Rv2965c, MT3043
ORF Names:MTCY349.22, u0002e
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

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 direct assay. Source: MTBBASE

protein hexamerization

Inferred from direct assay. Source: MTBBASE

   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 direct assay. Source: MTBBASE

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 161161Phosphopantetheine adenylyltransferase HAMAP MF_00151
PRO_0000156242

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A530 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: DE9F12E18D0C1721

FASTA16117,628
        10         20         30         40         50         60 
MTGAVCPGSF DPVTLGHVDI FERAAAQFDE VVVAILVNPA KTGMFDLDER IAMVKESTTH 

        70         80         90        100        110        120 
LPNLRVQVGH GLVVDFVRSC GMTAIVKGLR TGTDFEYELQ MAQMNKHIAG VDTFFVATAP 

       130        140        150        160 
RYSFVSSSLA KEVAMLGGDV SELLPEPVNR RLRDRLNTER T 

« Hide

References

« Hide 'large scale' references
[1]Smith D.R., Robison K.
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[3]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00024 Genomic DNA. Translation: AAA50946.1.
BX842581 Genomic DNA. Translation: CAB05412.1.
AE000516 Genomic DNA. Translation: AAK47369.1.
PIRB70671.
RefSeqNP_217481.1. NC_000962.2.
NP_337555.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TFUX-ray1.99A1-157[»]
3LCJX-ray2.10A1-161[»]
3NBAX-ray2.68A/B/C/D1-157[»]
3NBKX-ray1.58A/B/C/D1-157[»]
3PNBX-ray2.11A/B/C/D1-157[»]
ProteinModelPortalP0A530.
SMRP0A530. Positions 1-157.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000000913; EBMYCP00000000913; EBMYCG00000000913.
EBMYCT00000070721; EBMYCP00000068780; EBMYCG00000070716.
GeneID888423.
925233.
GenomeReviewsGene locus MT3043 in contig AE000516_GR.
Gene locus Rv2965c in contig AL123456_GR.
KEGGmtc:MT3043.
mtu:Rv2965c.
PATRIC18128450. VBIMycTub22151_3325.
TIGRMT3043.

Organism-specific databases

TubercuListRv2965c.

Phylogenomic databases

GeneTreeEBGT00050000017247.
HOGENOMHBG288308.
OMAAMSDFEY.
PhylomeDBP0A530.
ProtClustDBPRK00168.

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_MYCTU
AccessionPrimary (citable) accession number: P0A530
Secondary accession number(s): O08023, Q50452
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

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