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B8HQP9 (PROB_CYAP4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:Cyan7425_1670
OrganismCyanothece sp. (strain PCC 7425 / ATCC 29141) [Complete proteome] [HAMAP]
Taxonomic identifier395961 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesCyanothece

Protein attributes

Sequence length367 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 – 367367Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000193691

Regions

Domain275 – 35379PUA
Nucleotide binding168 – 1692ATP By similarity
Nucleotide binding210 – 2167ATP By similarity

Sites

Binding site81ATP By similarity
Binding site491Substrate By similarity
Binding site1361Substrate By similarity
Binding site1481Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B8HQP9 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: E6E3BE77A44922AF

FASTA36739,691
        10         20         30         40         50         60 
MTQTLVVKIG TSSLTHPKTG DLSLSTIAVL VETLSKLRRQ GQRIVLVSSG AVGVGCGRLG 

        70         80         90        100        110        120 
LSERPRTMAL KQAVAAVGQG RLMRIYDDFF TTLNQPIAQV LLTRGDLVQR QRYLNAYNTF 

       130        140        150        160        170        180 
QELFNLGVIP IVNENDTVAV DELKFGDNDT LSALVASLVE ADWLFLLTDV DRLYSADPRQ 

       190        200        210        220        230        240 
QPDAQPISVV NSIEELAQVQ VGDRGSIWGT GGMATKITAA EIAGEAGVRT VITEGRSPVN 

       250        260        270        280        290        300 
IERILAGEAL GTQFEPQPRP INARKRWIAH ALVPTGKLYL DRGAVQAIAQ LGKSLLAAGI 

       310        320        330        340        350        360 
VQVEGVFQSQ DAVLLCDRAG QEIGRGLVNY NSQELEKIQG RRSEEIPTIL GYSGAETVVH 


RDNLVLS 

« Hide

References

[1]"Novel metabolic attributes of the genus Cyanothece, comprising a group of unicellular nitrogen-fixing Cyanobacteria."
Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H., Sherman L.A., Pakrasi H.B.
MBio 2:E214-E214(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7425 / ATCC 29141.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001344 Genomic DNA. Translation: ACL44039.1.
RefSeqYP_002482400.1. NC_011884.1.

3D structure databases

ProteinModelPortalB8HQP9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395961.Cyan7425_1670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL44039; ACL44039; Cyan7425_1670.
GeneID7287593.
KEGGcyn:Cyan7425_1670.
PATRIC21564293. VBICyaSp30657_1667.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMARLMRAYE.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycCSP395961:GJDE-1489-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_CYAP4
AccessionPrimary (citable) accession number: B8HQP9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 40 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