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A5UDH4 (PROB_HAEIE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:CGSHiEE_07510
OrganismHaemophilus influenzae (strain PittEE) [Complete proteome] [HAMAP]
Taxonomic identifier374930 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length368 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 – 368368Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_1000081063

Regions

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

Sites

Binding site91ATP By similarity
Binding site491Substrate By similarity
Binding site1361Substrate By similarity
Binding site1481Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UDH4 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: E62B684193709836

FASTA36840,108
        10         20         30         40         50         60 
MNKKTIVVKF GTSTLTQGSP KLNSPHMMEI VRQIAQLHND GFRIVIVTSG AIAAGRHYLN 

        70         80         90        100        110        120 
HPQLPPTIAS KQLLAAVGQS QLIQAWEKLF AIYDIHIGQL LLTRADIEDR ERFLNARDTL 

       130        140        150        160        170        180 
HALLDNHIIP VINENDAVAT AEIKVGDNDN LSALVAILVQ AEQLYLLTDQ QGLFDSDPRK 

       190        200        210        220        230        240 
NPEAKLIPVV EQITDHIRSI AGGSGTNLGT GGMMTKIIAA DVATRSGIET IIAPGNRPNV 

       250        260        270        280        290        300 
IADLAYEQNI GTKFIAHQSD RLESRKQWLF AAPSAGIITI DNGAQNAILE QNKSLLPAGI 

       310        320        330        340        350        360 
INVEGRFSRG EVVKIRTQSG KDIALGMPRY NSDALQLIKG RKSADIENVL GYEYGAVAMH 


RDDMIILS 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittEE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000671 Genomic DNA. Translation: ABQ98825.1.
RefSeqYP_001291208.1. NC_009566.1.

3D structure databases

ProteinModelPortalA5UDH4.
SMRA5UDH4. Positions 2-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374930.CGSHiEE_07510.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ98825; ABQ98825; CGSHiEE_07510.
GeneID5225697.
KEGGhip:CGSHiEE_07510.
PATRIC20279159. VBIHaeInf81350_1513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
OMAMRMIAGH.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycHINF374930:GJDD-1390-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_HAEIE
AccessionPrimary (citable) accession number: A5UDH4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 10, 2007
Last modified: May 14, 2014
This is version 50 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