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Q6NFV9 (PROB_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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:DIP1777
OrganismCorynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]
Taxonomic identifier257309 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length376 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 – 376376Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109663

Regions

Domain284 – 35875PUA
Nucleotide binding182 – 1832ATP By similarity
Nucleotide binding222 – 2287ATP By similarity

Sites

Binding site231ATP By similarity
Binding site631Substrate By similarity
Binding site1501Substrate By similarity
Binding site1621Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NFV9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: B48316665C25E7B0

FASTA37639,361
        10         20         30         40         50         60 
MNAQHSSADL RDVIRNAKRI VVKIGSSSLT GENFEVSPGR IDRIVEALED RMHRGSDVIV 

        70         80         90        100        110        120 
VSSGAVAAGM APLGLTSRPK DLATKQAAAS VGQVHLANAW GNSFARYNRT IGQVLLTASD 

       130        140        150        160        170        180 
AGQRDRARNA QRTIDRLRLL HAVPIINEND TVATSEMHFG DNDRLAAIVS HLVSADALVL 

       190        200        210        220        230        240 
LSDVDGLYDK NPADPSARFV SEVRDGNDLK GVIAGDGGAV GTGGMASKVS AARLASRSGV 

       250        260        270        280        290        300 
PVLLTSADYV AEALGDAEVG TVFYPKDDRL SAWKFWALYA ADTGGALRID AGAVAAVTAG 

       310        320        330        340        350        360 
GNSLLAVGIT EVIGDFHAGE IVEILGPEGE IIGRGEVAYD SAVLITMLGK QTAQLPEGLQ 

       370 
RPVVHADYLS DYASRA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248359 Genomic DNA. Translation: CAE50307.1.
RefSeqNP_940115.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NFV9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257309.DIP1777.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE50307; CAE50307; DIP1777.
GeneID2649402.
KEGGcdi:DIP1777.
PATRIC21484780. VBICorDip47633_1763.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

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_CORDI
AccessionPrimary (citable) accession number: Q6NFV9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 71 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