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Q1BAN0 (Q1BAN0_MYCSS) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphopantetheine adenylyltransferase HAMAP MF_00151
EC=2.7.7.3 HAMAP MF_00151
Alternative name(s):
Dephospho-CoA pyrophosphorylase HAMAP MF_00151
Pantetheine-phosphate adenylyltransferase HAMAP MF_00151
Gene names
Name:coaD HAMAP MF_00151
Ordered Locus Names:Mmcs_1945
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length170 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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. HAMAP MF_00151

Sequences

Sequence LengthMass (Da)Tools
Q1BAN0 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 465526A468614691

FASTA17018,311
        10         20         30         40         50         60 
MTPDLDRVRS SPMSGAVCPG SFDPVTLGHV DIFERAAAQF DEVVVAVLVN PNKKGMFTLD 

        70         80         90        100        110        120 
ERMEMIAESC AHLPNLRVES GQGLVVDFVR ARGYSAIVKG LRSSTDFEYE LQMAQMNKHV 

       130        140        150        160        170 
AGVDTFFIAS APSYSFVSSS LAKEVATLGG DVSALLPDAV NVRLQAKLRG

« Hide

References

[1]"Complete sequence of chromosome of Mycobacterium sp. MCS."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000384 Genomic DNA. Translation: ABG08054.1.
RefSeqYP_639110.1. NC_008146.1.

3D structure databases

ProteinModelPortalQ1BAN0.
SMRQ1BAN0. Positions 13-168.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1BAN0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000061669; EBMYCP00000059836; EBMYCG00000061664.
GeneID4110779.
GenomeReviewsGene locus Mmcs_1945 in contig CP000384_GR.
KEGGmmc:Mmcs_1945.
PATRIC18114071. VBIMycSp106721_1989.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0669.
GeneTreeEBGT00050000017247.
HOGENOMHBG288308.
OMAAMSDFEY.
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 nameQ1BAN0_MYCSS
AccessionPrimary (citable) accession number: Q1BAN0
Entry history
Integrated into UniProtKB/TrEMBL: July 11, 2006
Last sequence update: July 11, 2006
Last modified: December 14, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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