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Q5QY57 (PROB_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:IL1985
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

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.

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_0000109681

Regions

Domain275 – 35480PUA
Nucleotide binding168 – 1692ATP By similarity
Nucleotide binding210 – 2167ATP By similarity

Sites

Binding site121ATP By similarity
Binding site521Substrate By similarity
Binding site1361Substrate By similarity
Binding site1481Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QY57 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: C4FCFDDE0D5CA064

FASTA37140,588
        10         20         30         40         50         60 
MKAPSWRRAV LKVGSALIAP DETGVSTKYL LPIARFINEC RERGQEVVLV SSGSVAAGRK 

        70         80         90        100        110        120 
HFNFEHKKVP VAVRKAMSAV GQNEMMGYWS RFFDSPCAQL LMTHSDLRDR ARYVSIKNTL 

       130        140        150        160        170        180 
NRLLEHDILP VVNENDALAT DEMKVGDNDN LSAMIATLVD ADALFICSDI DGLYDSDPNL 

       190        200        210        220        230        240 
NPDAKKIPVV EQIDESIYSL AGGSVSSVGT GGMRTKVEAA EKATSHGIDT YIVNGRKGET 

       250        260        270        280        290        300 
FESLLQGDIP GTLFRRQSDP ISNKKHWLRH TLVAQGEILV DEGAEKALIE NGASLLSSGI 

       310        320        330        340        350        360 
VDVQGDFDRG DAVLVRSAND TDAIAKGICQ YSAHELMHIK GQQTEDIAEK FGYSPITEVI 

       370 
HRDDLMILED S 

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV82817.1.
RefSeqYP_156366.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QY57.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL1985.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV82817; AAV82817; IL1985.
GeneID3173759.
KEGGilo:IL1985.
PATRIC22142108. VBIIdiLoi21852_1996.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAAQNAGCT.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycILOI283942:GI0U-1999-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.
IPR004521. Uncharacterised_CHP00451.
[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.
TIGR00451. unchar_dom_2. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_IDILO
AccessionPrimary (citable) accession number: Q5QY57
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: January 4, 2005
Last modified: February 19, 2014
This is version 63 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