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Q3IXX8 (PROB_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. 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:RHOS4_30380
ORF Names:RSP_3823
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length370 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
Reference 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 – 370370Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000230063

Regions

Domain280 – 35778PUA
Nucleotide binding175 – 1762ATP By similarity

Sites

Binding site171ATP By similarity
Binding site561Substrate By similarity
Binding site1431Substrate By similarity
Binding site1551Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IXX8 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 23B55E2BF1EB91B4

FASTA37038,960
        10         20         30         40         50         60 
MPLQAPDIRS AKRLVVKIGS ALLVDGEGLR RQWLSALALD VAEARTRGTQ VILVSSGSIA 

        70         80         90        100        110        120 
LGRRVLHLPP GPLALEQSQA AAAVGQIRLA RAYEEVLAPH GITTAQVLVT LEDTEDRRRY 

       130        140        150        160        170        180 
LNSRATMETL LGLGTVPIVN ENDTVATDEI RFGDNDRLAA QIAVTVGADQ LVLLSDVDGF 

       190        200        210        220        230        240 
YSANPKEDPT AERFDLVETI TPALEAMAGD PVSGLSKGGM KTKIMAAKTA VAGGCAMAIT 

       250        260        270        280        290        300 
EGSAMRPLKA LEQGAARTWF VAQGDPQAAR KRWINAMKPR GTIRVDAGAV QALQAGKSLL 

       310        320        330        340        350        360 
PAGVVAVEGN FGRGDPVEIA GPMGEVLGRG LTRYTAVEAV QIAGHRSAEI VAILGYSGRA 

       370 
ALIHRDDMVI 

« Hide

References

[1]"Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000144 Genomic DNA. Translation: ABA80606.1.
RefSeqYP_354507.1. NC_007494.2.

3D structure databases

ProteinModelPortalQ3IXX8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272943.RSP_3823.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA80606; ABA80606; RSP_3823.
GeneID3721404.
KEGGrsp:RSP_3823.
PATRIC23156108. VBIRhoSph57909_3409.

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAIDGLYSC.
OrthoDBEOG6PGK7G.
PhylomeDBQ3IXX8.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-3116-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_RHOS4
AccessionPrimary (citable) accession number: Q3IXX8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: July 9, 2014
This is version 60 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