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Q7U842 (PROB_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 67. 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:SYNW0782
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length357 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 – 357357Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109744

Regions

Domain270 – 34778PUA
Nucleotide binding162 – 1632ATP By similarity

Sites

Binding site71ATP By similarity
Binding site431Substrate By similarity
Binding site1301Substrate By similarity
Binding site1421Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7U842 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: D5F7C167492CB2DF

FASTA35737,355
        10         20         30         40         50         60 
MTLWVVKLGT SLLRGDTAAT IAGFAAGIAA AFARGDRVVL VSSGAVGLGC QRLQLPQRPE 

        70         80         90        100        110        120 
TVVALQAAAA TGQGQLMALY ERALANHGIA VAQILVTRSD LADRRRYQNA SGTLQQLLQW 

       130        140        150        160        170        180 
GVLPVVNEND AISPAELRFG DNDTLSALVA AAVGADQLIL LTDVDRLYSA DPRLVVDARP 

       190        200        210        220        230        240 
ISDVHHPREL DALEAVAGDG GRWGRGGMTT KLAAARIATA SGITVHLADG RDPRRLDALL 

       250        260        270        280        290        300 
QGERGGTVFH PHPEPLGNRR SWLAHALQPQ GELTLDAGAC DALHQRGSSL LMVGITAVKG 

       310        320        330        340        350 
VFGANQPVRL QGPDGRELGR GLCQLSSAAV QRALDAAPAA GPSPVVVHRD ALVLHSR 

« Hide

References

[1]"The genome of a motile marine Synechococcus."
Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.
Nature 424:1037-1042(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH8102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX569691 Genomic DNA. Translation: CAE07297.1.
RefSeqNP_896875.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7U842.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING84588.SYNW0782.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE07297; CAE07297; SYNW0782.
GeneID1731688.
KEGGsyw:SYNW0782.
PATRIC23833005. VBISynSp27240_0810.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

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_SYNPX
AccessionPrimary (citable) accession number: Q7U842
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2003
Last modified: May 14, 2014
This is version 67 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