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Q2JNZ0 (PROB_SYNJB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:CYB_0519
OrganismSynechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) [Complete proteome] [HAMAP]
Taxonomic identifier321332 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length371 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.

Sequence caution

The sequence ABD01511.1 differs from that shown. Reason: Erroneous initiation.

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 – 371371Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000253010

Regions

Domain278 – 35679PUA
Nucleotide binding171 – 1722ATP By similarity
Nucleotide binding213 – 2197ATP By similarity

Sites

Binding site111ATP By similarity
Binding site521Substrate By similarity
Binding site1391Substrate By similarity
Binding site1511Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2JNZ0 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: E07F1B95CD49D42C

FASTA37139,356
        10         20         30         40         50         60 
MATTDVTVVV KIGTSSLTDT QTGLLRLSVL GPLVEVLTHL RRQGYAVILV SSGAVGVGCA 

        70         80         90        100        110        120 
RLGWRQRPTA IAEKQAVAAV GQGRLIRLYD DLFSALNQPI AQVLLTRGDL VERSRYVNAN 

       130        140        150        160        170        180 
RTFAQLLQMG VIPIVNENDT VAVEELKFGD NDSLSALVAS MVQAKWLILL TDVDKLYSAD 

       190        200        210        220        230        240 
PNRDPSAQPI ERVLPGIPLQ VKAEAQGKSG WGTGGMATKL TAAQIATAAG VTVVITNGKR 

       250        260        270        280        290        300 
PEQIPAILAG EAIGTRFDPA PQPASARKRW IAYGLIPEGS LTLDEGAVRA VCEQGRSLLP 

       310        320        330        340        350        360 
AGITAISGEF EAGAAVRLCD PSGQEVARGL VNYSAEELRQ IKGKKTAEIP RILGYEGVDT 

       370 
AVHRDNLALL N 

« Hide

References

[1]"Population level functional diversity in a microbial community revealed by comparative genomic and metagenomic analyses."
Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.
ISME J. 1:703-713(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JA-2-3B'a(2-13).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000240 Genomic DNA. Translation: ABD01511.1. Different initiation.
RefSeqYP_476774.1. NC_007776.1.

3D structure databases

ProteinModelPortalQ2JNZ0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING321332.CYB_0519.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD01511; ABD01511; CYB_0519.
GeneID3900497.
KEGGcyb:CYB_0519.
PATRIC23803328. VBISynSp29577_0526.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycSSP321332:GH1B-519-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_SYNJB
AccessionPrimary (citable) accession number: Q2JNZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 58 of the entry and version 2 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