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Reviewed, UniProtKB/Swiss-Prot Q8NRQ2 (COAA_CORGL)

Last modified June 16, 2009. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pantothenate kinase
    EC=2.7.1.33
Alternative name(s):
    Pantothenic acid kinase
Gene names
Name: coaA
Ordered Locus Names: Cgl0995, cg1132
OrganismCorynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate. HAMAP MF_00215

Pathway

Cofactor biosynthesis; coenzyme A biosynthesis; coenzyme A from pantothenate: step 1/5. HAMAP MF_00215

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the prokaryotic pantothenate kinase family.

Ontologies

Keywords
   Biological processCoenzyme A biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcoenzyme A biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

pantothenate kinase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Pantothenate kinase HAMAP MF_00215
PRO_0000194424

Regions

Nucleotide binding97 – 1048ATP Potential

Sequences

Sequence LengthMass (Da)Tools
Q8NRQ2-1 [UniParc].

Last modified October 10, 2002. Version 1.
Checksum: BBDE9EF3C83F95F6

FASTA31235,316
        10         20         30         40         50         60 
MKPSPRTPDF SPYLDFDRAQ WRELRNSMPQ VLTQKEVIEL RGIGENIDLA EVAEVYLPLS 

        70         80         90        100        110        120 
RLIHLQVAAR QQLTAATETF LGTSPSISVP FVIGVAGSVA VGKSTTARLL QVLLQRWNSH 

       130        140        150        160        170        180 
PRVDLVTTDG FLYPGAELIR RGLMSRKGFP ESYDQRALLR FVTDVKSGKL EVNAPVYSHT 

       190        200        210        220        230        240 
AYDRVPGEFT TVRQPDILIV EGLNVLQTGP TLMVSDLFDF SVYVDARTED IEKWYIDRFL 

       250        260        270        280        290        300 
KLRDTAFRRP GAHFSHYADM ADPESIAVAR ELWQSINLPN LVENILPTRV RASLVLKKGS 

       310 
DHLVERVRMR KI 

« 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.

Cross-references

Sequence databases

BA000036 Genomic DNA. Translation: BAB98388.1.
BX927151 Genomic DNA. Translation: CAF19699.1. Different initiation.
RefSeqNP_600220.1.
YP_225285.1.

3D structure databases

HSSPHSSP built from PDB template 1ESM based on UniProtKB P15044.
ModBaseSearch...

Genome annotation databases

GeneID1018982.
3342901.
GenomeReviewsGene locus Cgl0995 in contig BA000036_GR.
Gene locus cg1132 in contig BX927147_GR.
KEGGcgb:cg1132.
cgl:NCgl0953.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8NRQ2.
OMAQ8NRQ2. PKVDLIT.

Enzyme and pathway databases

BioCycCGLU196627-1:CG1132-MON.
BRENDA2.7.1.33. 812.

Family and domain databases

HAMAPMF_00215.
[Tree]
InterProIPR004566. PanK_bact.
[Graphical view]
PANTHERPTHR10285:SF7. PanK_bact. 1 hit.
PIRSFPIRSF000545. Pantothenate_kin. 1 hit.
TIGRFAMsTIGR00554. panK_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCOAA_CORGL
AccessionPrimary (citable) accession number: Q8NRQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 10, 2002
Last modified: June 16, 2009
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents