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Q8CUQ5 (PROB_OCEIH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. 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:OB1052
OrganismOceanobacillus iheyensis (strain DSM 14371 / JCM 11309 / KCTC 3954 / HTE831) [Complete proteome] [HAMAP]
Taxonomic identifier221109 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeOceanobacillus

Protein attributes

Sequence length372 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 – 372372Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109701

Regions

Domain276 – 36085PUA
Nucleotide binding168 – 1692ATP By similarity
Nucleotide binding210 – 2167ATP By similarity

Sites

Binding site91ATP By similarity
Binding site491Substrate By similarity
Binding site1361Substrate By similarity
Binding site1481Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CUQ5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 93C879B29BB36FF7

FASTA37240,618
        10         20         30         40         50         60 
MNKKRVVIKI GSSSLTNEKG EIDHKKLGDH VNALAMLHQH NFEVILVSSG AVAAGFRNLG 

        70         80         90        100        110        120 
YSSRPVTLKG KQASAAIGQG LLIHTYMDKF MEYNIRSAQL LLTRSDFSVQ KRYKNATSTM 

       130        140        150        160        170        180 
LELLERGVIP IINENDTVAV DELTFGDNDM LSALVSGSIH AAQLIILTDI DGIYDKHPGK 

       190        200        210        220        230        240 
YASAMRYDTI DLITNDMIQE TDVSGSKLGT GGMKSKLMAA KVAASLGVPV FIGKGVGVSK 

       250        260        270        280        290        300 
LLEIVNGHGQ GTYVRSFRNK QIPIRKQWIS LHSTLEGKVF IDDGATQALM HNGGSLLSAG 

       310        320        330        340        350        360 
VINTQGDFED GDVVEVYNRR NLLGRGQVSC SSEELNAANT LKKAKQMTQI PAIEVIHRDS 

       370 
WVMVDQIKEE FQ 

« Hide

References

[1]"Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments."
Takami H., Takaki Y., Uchiyama I.
Nucleic Acids Res. 30:3927-3935(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000028 Genomic DNA. Translation: BAC13008.1.
RefSeqNP_691973.1. NC_004193.1.

3D structure databases

ProteinModelPortalQ8CUQ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING221109.OB1052.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC13008; BAC13008; BAC13008.
GeneID1016930.
KEGGoih:OB1052.
PATRIC22793102. VBIOceIhe82024_1069.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycOIHE221109:GI2A-1128-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_OCEIH
AccessionPrimary (citable) accession number: Q8CUQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 73 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