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Q0AHG4 (PROB_NITEC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:Neut_0958
OrganismNitrosomonas eutropha (strain C91) [Complete proteome] [HAMAP]
Taxonomic identifier335283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length373 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 – 373373Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000081081

Regions

Domain281 – 35979PUA
Nucleotide binding174 – 1752ATP By similarity

Sites

Binding site151ATP By similarity
Binding site551Substrate By similarity
Binding site1421Substrate By similarity
Binding site1541Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AHG4 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 7BBA6B28864D12F3

FASTA37340,016
        10         20         30         40         50         60 
MTRSILQSAR RIIVKVGSSL VTNEGSGLDR QVLGGWAGQI SRLKKMGKEV VLVSSGAVAE 

        70         80         90        100        110        120 
GMQRLGWKTR PAALYELQAA AAVGQMDLAQ AYADCFSEYK LLTAQILLTH DDLSSRKRYL 

       130        140        150        160        170        180 
NARSTILTLL NLDIVPIINE NDTVVSDEIR FGDNDNLAAL VANLIEAEVL VILTDQEGLF 

       190        200        210        220        230        240 
TGDPRKHADA TLISEISVSD PHIETMAGGT SSGIGRGGMQ SKVMAARRAA RSGAHTVIAS 

       250        260        270        280        290        300 
GRVENVLVRL ANGEAIGTSL LADMPVKVAR KLWLADHLQV RGSVVLDDGA SRALLSGGKS 

       310        320        330        340        350        360 
LLPIGVVEVR GNFERGEAIS CLNTSGREIA RGLANYSARE SHKIMRRPSS QIEAVLGYVG 

       370 
EYELVHRDNL VIL 

« Hide

References

[1]"Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C91.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000450 Genomic DNA. Translation: ABI59218.1.
RefSeqYP_747183.1. NC_008344.1.

3D structure databases

ProteinModelPortalQ0AHG4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335283.Neut_0958.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI59218; ABI59218; Neut_0958.
GeneID4272429.
KEGGnet:Neut_0958.
PATRIC22719105. VBINitEut7577_1219.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMATVIHRDN.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycNEUT335283:GHT6-978-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_NITEC
AccessionPrimary (citable) accession number: Q0AHG4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 17, 2006
Last modified: February 19, 2014
This is version 54 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