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B4RD63 (PROB_PHEZH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 42. 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:PHZ_c0253
OrganismPhenylobacterium zucineum (strain HLK1) [Complete proteome] [HAMAP]
Taxonomic identifier450851 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaCaulobacteralesCaulobacteraceaePhenylobacterium

Protein attributes

Sequence length375 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 – 375375Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000125247

Regions

Domain280 – 35778PUA
Nucleotide binding172 – 1732ATP By similarity
Nucleotide binding216 – 2227ATP By similarity

Sites

Binding site131ATP By similarity
Binding site531Substrate By similarity
Binding site1401Substrate By similarity
Binding site1521Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B4RD63 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 525A07371ED186E7

FASTA37538,733
        10         20         30         40         50         60 
MSGLGQARRV VVKVGSALLV GPDGAPHADW LADFAADAAR MRARGQQVLV VSSGAVALGR 

        70         80         90        100        110        120 
RRLGLARRAL TLPEKQAAAA AGQSALMRAW EEAFEPHGAA CAQVLLTRDD TEVRRRWLNA 

       130        140        150        160        170        180 
RATVETLLGL GVVPVINEND TVVTEEIRYG DNDRLAARVA QLVGADVLVL LSDVDGLYTA 

       190        200        210        220        230        240 
DPRKDPAARH IPRVPRLTPE VEAMAGGANA EGGVGTGGMA TKIAAARIAA AGGCATVITL 

       250        260        270        280        290        300 
GSRTRPLAAV EGGERATVVE PATTPAAAYK AWIAGSLAPA GALVVDDGAA QAVRRGKSLL 

       310        320        330        340        350        360 
AAGVRRVEGR FDKGDAVLVR DEAGREIARG LVRYEAADAE RICGLKSEAI EGVLGYTSGP 

       370 
LVHADDLALA AHAEA 

« Hide

References

[1]"Complete genome of Phenylobacterium zucineum - a novel facultative intracellular bacterium isolated from human erythroleukemia cell line K562."
Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.
BMC Genomics 9:386-386(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HLK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000747 Genomic DNA. Translation: ACG76667.1.
RefSeqYP_002129096.1. NC_011144.1.

3D structure databases

ProteinModelPortalB4RD63.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING450851.PHZ_c0253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACG76667; ACG76667; PHZ_c0253.
GeneID6789743.
KEGGpzu:PHZ_c0253.
PATRIC22923060. VBIPheZuc44517_0625.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAHGEISIR.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycPZUC450851:GHUG-257-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_PHEZH
AccessionPrimary (citable) accession number: B4RD63
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 23, 2008
Last modified: May 14, 2014
This is version 42 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