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Q92LB3 (PROB1_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 79. 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 1

EC=2.7.2.11
Alternative name(s):
Gamma-glutamyl kinase 1
Short name=GK 1
Gene names
Name:proB1
Ordered Locus Names:R03160
ORF Names:SMc03776
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length393 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 – 393393Glutamate 5-kinase 1 HAMAP-Rule MF_00456
PRO_0000109715

Regions

Domain282 – 35978PUA
Nucleotide binding176 – 1772ATP By similarity

Sites

Binding site171ATP By similarity
Binding site571Substrate By similarity
Binding site1441Substrate By similarity
Binding site1561Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92LB3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2424B9FEDDEF9C22

FASTA39340,869
        10         20         30         40         50         60 
MTKARKALEN YRRVVIKIGS ALLVDRRTGL KKSWLDALCA DIAALRAKGV EVLVVSSGAI 

        70         80         90        100        110        120 
ALGRTVLDLP AGALKLEESQ AAAAVGQIVL ARAWSESLST HAIVAGQILL TLGDTEERRR 

       130        140        150        160        170        180 
YLNARATIGQ LLKLGSVPII NENDTVATTE IRYGDNDRLA ARVATMVGAD LLVLLSDIDG 

       190        200        210        220        230        240 
LYTAPPHLDP NARFLETVAE ITPEIEAMAG GAASELSRGG MRTKIDAGKI ATTAGCAMII 

       250        260        270        280        290        300 
ASGKPDHPLA AIEAGARSSW FAPSGSPVTA RKTWIAGQLL PAGSLSIDAG AETALRSGKS 

       310        320        330        340        350        360 
LLPAGVRQVT GSFSRGDTIA IIGASGREIA RGLAGYDADE ARQIAGKKSA EIAAILGYAG 

       370        380        390 
RTAMVHRDDL VMTAPSGARL VEESDEGKGK LHA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL591688 Genomic DNA. Translation: CAC47739.1.
RefSeqNP_387266.1. NC_003047.1.

3D structure databases

ProteinModelPortalQ92LB3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc03776.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC47739; CAC47739; SMc03776.
GeneID1234853.
KEGGsme:SMc03776.
PATRIC23635970. VBISinMel96828_4708.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMATVIHRDN.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-3248-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 namePROB1_RHIME
AccessionPrimary (citable) accession number: Q92LB3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 79 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