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Q2G982 (PROB_NOVAD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:Saro_1146
OrganismNovosphingobium aromaticivorans (strain DSM 12444) [Complete proteome] [HAMAP]
Taxonomic identifier279238 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium

Protein attributes

Sequence length377 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 – 377377Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252989

Regions

Domain286 – 36378PUA
Nucleotide binding181 – 1822ATP By similarity
Nucleotide binding223 – 2297ATP By similarity

Sites

Binding site211ATP By similarity
Binding site611Substrate By similarity
Binding site1491Substrate By similarity
Binding site1611Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2G982 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 7B461C0427B8B72C

FASTA37738,909
        10         20         30         40         50         60 
MKISQLAQLT QASTCPRLVV KVGSALLVGK DGEPRREWLS ALVSEIAAMR AAGQEVIVVS 

        70         80         90        100        110        120 
SGAIALGARK LGLAKGGRGS LSDAQAAASV GQIALAGLWA ELLAQHGLTA AQILLTLEDL 

       130        140        150        160        170        180 
EDRRRYLNVT ATLGTLLAAC AVPVINENDS VATQEIRFGD NDRLAARVGQ AAGASGVLLL 

       190        200        210        220        230        240 
SDIDGLYDRD PRQPGATRIP VVKGVTPEIH AMATGGSSSG LGSGGMTSKL QAAEIAELAG 

       250        260        270        280        290        300 
MALAIIDGQP VAPIAAAMGA ARGTLFLPRG RKQARKAWLG GRMRMRGSVQ VDAGAAAALA 

       310        320        330        340        350        360 
RGSSLLAAGV TEVDGDFQRG DAIAVLGPDG RTLARGLSEY DAAECARLKG RHSREHEELL 

       370 
GYAPRSALIH RDQMVLL 

« Hide

References

[1]"Complete sequence of Novosphingobium aromaticivorans DSM 12444."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N. expand/collapse author list , Fredrickson J., Balkwill D., Romine M.F., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 12444.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000248 Genomic DNA. Translation: ABD25591.1.
RefSeqYP_496425.1. NC_007794.1.

3D structure databases

ProteinModelPortalQ2G982.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279238.Saro_1146.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD25591; ABD25591; Saro_1146.
GeneID3916443.
KEGGnar:Saro_1146.
PATRIC22784928. VBINovAro50627_1168.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycNARO279238:GHBU-1161-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_NOVAD
AccessionPrimary (citable) accession number: Q2G982
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: March 21, 2006
Last modified: February 19, 2014
This is version 59 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