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Q9ZG98 (PROB_MEIRU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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
OrganismMeiothermus ruber
Taxonomic identifier277 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeMeiothermus

Protein attributes

Sequence length377 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 AAC72812.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
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 – 377377Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109691

Regions

Domain281 – 35979PUA
Nucleotide binding174 – 1752ATP By similarity
Nucleotide binding216 – 2227ATP By similarity

Sites

Binding site181ATP By similarity
Binding site551Substrate By similarity
Binding site1421Substrate By similarity
Binding site1541Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZG98 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: F637DFE9DD811155

FASTA37740,592
        10         20         30         40         50         60 
MHGRLPLTAQ THRRLVVKVG SAVLSGPQGR QHQLAIAAQV AALRAEGREV VLVSSGAQAT 

        70         80         90        100        110        120 
GMQKLGLTEK PKSMPGKQAL AAVGQPTLML LWEQAFSWYD LKVAQVLLTA EDLAHRHRYL 

       130        140        150        160        170        180 
NARQTLETLL EWGIVPIINE NDTVMVEEIK FGDNDQLSAL IASLVGADLL ILLSDIEALY 

       190        200        210        220        230        240 
EADPRTHPEA QPIPYVERVD AGVLRMAGDS PNRVGTGGMK SKLLAAEKAQ AAGIPHLLLP 

       250        260        270        280        290        300 
GTRPQSIAEA LQGAPVGTLF AGGQRRYSGR KLWLYQLPKP QGEVVVDAGA AKALRQGGAS 

       310        320        330        340        350        360 
LLPAGILEVR GQFGVGEAVR CLDEQGNLIG VGLVNYSAAE LARIKRRKTR EIEALLGYKN 

       370 
TDEAIHRDYF ALASELE 

« Hide

References

[1]"Molecular cloning and sequence analysis of the proA gene from thermophilic eubacterium Thermus ruber."
Yaklichkin S.Y., Zimina M.S., Yurchenko Y.V., Hromov I.S., Neumivakin L.V.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF082661 Genomic DNA. Translation: AAC72812.1. Different initiation.

3D structure databases

ProteinModelPortalQ9ZG98.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_MEIRU
AccessionPrimary (citable) accession number: Q9ZG98
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 26, 2001
Last modified: February 19, 2014
This is version 67 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