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A0PU14 (PROB_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 57. 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:
Glutamate 5-kinase

EC=2.7.2.11
Alternative name(s):
Gamma-glutamyl kinase
Short name=GK
Gene names
Name:proB
Ordered Locus Names:MUL_3711
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline By similarity. HAMAP-Rule MF_00456

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP-Rule MF_00456

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP-Rule MF_00456

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00456.

Sequence similarities

Belongs to the glutamate 5-kinase family.

Contains 1 PUA domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: InterPro

glutamate 5-kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000081078

Regions

Domain280 – 35879PUA
Nucleotide binding177 – 1782ATP By similarity
Nucleotide binding218 – 2247ATP By similarity

Sites

Binding site181ATP By similarity
Binding site581Substrate By similarity
Binding site1451Substrate By similarity
Binding site1571Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PU14 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 0026A0DD4F336759

FASTA36837,963
        10         20         30         40         50         60 
MGSPHREAIR TARSVVVKVG TTALTTPSGV FDAGRLAELA DAIESRMKAG TDVVIVSSGA 

        70         80         90        100        110        120 
IAAGIEPLGL SRRPKDLATK QAAASVGQVA LVNSWSAAFA RYGRTVGQVL LTAHDIAMRV 

       130        140        150        160        170        180 
QHTNAQRTLD RLRALHAVGI VNENDTVATN EIRFGDNDRL SALVAHLVGA DALVLLSDID 

       190        200        210        220        230        240 
GLYDADPRKF QNARFIPEVS GPADLDGVVA GQGSHLGTGG MASKMSSALL AADAGVPVLL 

       250        260        270        280        290        300 
APAADAAAAL TDASVGTVFA ARSERMSARR FWVRYAAESA GSLTLDEGAV RAVVGHRRSL 

       310        320        330        340        350        360 
LPAGITAVAG KFFGGDVVDL CGPDATMVAR GVVAYDATEL AAMMGRSTSE LPGELRRPAV 


HADDLVAV 

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000325 Genomic DNA. Translation: ABL05833.1.
RefSeqYP_907304.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PU14.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362242.MUL_3711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL05833; ABL05833; MUL_3711.
GeneID4553004.
KEGGmul:MUL_3711.
PATRIC18175011. VBIMycUlc37413_4328.

Organism-specific databases

GenoListMUL_3711.
CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

UniPathwayUPA00098; UER00359.

Family and domain databases

Gene3D2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPMF_00456. ProB.
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR011529. Glu_5kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view]
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_MYCUA
AccessionPrimary (citable) accession number: A0PU14
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 9, 2007
Last modified: February 19, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways