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Q3AYS3 (PROB_SYNS9) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:Syncc9902_0786
OrganismSynechococcus sp. (strain CC9902) [Complete proteome] [HAMAP]
Taxonomic identifier316279 [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_0000253009

Regions

Domain270 – 34172PUA
Nucleotide binding162 – 1632ATP By similarity
Nucleotide binding205 – 2117ATP 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
Q3AYS3 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 2D15989D9FBF5732

FASTA35737,722
        10         20         30         40         50         60 
MTLWVVKLGT SLLRGDTAAT IEGYASGLAA AMRRGDQVVL VTSGAVGLGC QKLHLPKRPD 

        70         80         90        100        110        120 
TVVALQAAAA TGQGYLMALY ERAMAVHGLS VAQVLLTRSD LVDRRRYQNA SGTLQQLLAW 

       130        140        150        160        170        180 
GVLPVINEND ALSSAELRFG DNDTLSALVA AAVGAHQLLL LTDVDRLYSS DPRSDANAQP 

       190        200        210        220        230        240 
ITDVHHPRDL KWLEAGAGDG GRWGTGGMTT KLAAARIATA SGVTVHLADG RDPARLAGLL 

       250        260        270        280        290        300 
EGDRGGTVFH PHPEPLGNRR SWLAHVLVPE GELCLDQGAC QALLHRGASL LLVGVTAVKG 

       310        320        330        340        350 
QFEANRPVLL RDPDGQELGR GLCTLNSNQV RQALSVVTDA EASPVVVHRD ALVLQDR 

« Hide

References

[1]"Complete sequence of Synechococcus sp. CC9902."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CC9902.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000097 Genomic DNA. Translation: ABB25754.1.
RefSeqYP_376798.1. NC_007513.1.

3D structure databases

ProteinModelPortalQ3AYS3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316279.Syncc9902_0786.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB25754; ABB25754; Syncc9902_0786.
GeneID3743893.
KEGGsye:Syncc9902_0786.
PATRIC23798793. VBISynSp76179_0860.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycSSP316279:GJCI-798-MONOMER.
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_SYNS9
AccessionPrimary (citable) accession number: Q3AYS3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 61 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