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Q8NQU5 (COAD_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Ordered Locus Names:Cgl1329, cg1501
OrganismCorynebacterium glutamicum (Brevibacterium flavum)
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length160 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 termComplete 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 – 160160Phosphopantetheine adenylyltransferase HAMAP MF_00151
PRO_0000156199

Sequences

Sequence LengthMass (Da)Tools
Q8NQU5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 26B342D93E9DC2FC

FASTA16017,575
        10         20         30         40         50         60 
MKAVCPGSFD PITLGHLDIV TRAAAQFSEV TILVTANPNK NSGLFTVAER MDLIRESTAH 

        70         80         90        100        110        120 
LDNVKVDTWA SLLVDYTTEH GIGALVKGLR SSLDYEYELP MAQMNRRLTG VDTFFLLTDE 

       130        140        150        160 
KYGYVSSTLC KEVARFGGDV SGLLPEVVAK AVTEKYSNQH 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000036 Genomic DNA. Translation: BAB98722.1.
BX927151 Genomic DNA. Translation: CAF20027.1.
RefSeqNP_600549.1. NC_003450.3.
YP_225613.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ8NQU5.
SMRQ8NQU5. Positions 2-157.
ModBaseSearch...

2D gel databases

World-2DPAGE0001:Q8NQU5.

Proteomic databases

PRIDEQ8NQU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1019305.
3345017.
GenomeReviewsGene locus Cgl1329 in contig BA000036_GR.
Gene locus cg1501 in contig BX927147_GR.
KEGGcgb:cg1501.
cgl:NCgl1275.
PATRIC21494697. VBICorGlu203724_1299.

Phylogenomic databases

HOGENOMHBG288308.
OMAAMSDFEY.
PhylomeDBQ8NQU5.
ProtClustDBPRK00168.

Enzyme and pathway databases

BioCycCGLU196627:CG1501-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_CORGL
AccessionPrimary (citable) accession number: Q8NQU5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 55 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

SIMILARITY comments

Index of protein domains and families