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A5U5D5 (PROB_MYCTA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. 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:MRA_2465
OrganismMycobacterium tuberculosis (strain ATCC 25177 / H37Ra) [Complete proteome] [HAMAP]
Taxonomic identifier419947 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

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 MF_00456

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP MF_00456

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP MF_00456

Subcellular location

Cytoplasm By similarity HAMAP 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 processproline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376Glutamate 5-kinase HAMAP MF_00456
PRO_1000081077

Regions

Domain280 – 35879PUA

Sequences

Sequence LengthMass (Da)Tools
A5U5D5 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: AC7BB66C0B302E6A

FASTA37638,788
        10         20         30         40         50         60 
MRSPHRDAIR TARGLVVKVG TTALTTPSGM FDAGRLAGLA EAVERRMKAG SDVVIVSSGA 

        70         80         90        100        110        120 
IAAGIEPLGL SRRPKDLATK QAAASVGQVA LVNSWSAAFA RYGRTVGQVL LTAHDISMRV 

       130        140        150        160        170        180 
QHTNAQRTLD RLRALHAVAI VNENDTVATN EIRFGDNDRL SALVAHLVGA DALVLLSDID 

       190        200        210        220        230        240 
GLYDCDPRKT ADATFIPEVS GPADLDGVVA GRSSHLGTGG MASKVAAALL AADAGVPVLL 

       250        260        270        280        290        300 
APAADAATAL ADASVGTVFA ARPARLSARR FWVRYAAEAT GALTLDAGAV RAVVRQRRSL 

       310        320        330        340        350        360 
LAAGITAVSG RFCGGDVVEL RAPDAAMVAR GVVAYDASEL ATMVGRSTSE LPGELRRPVV 

       370 
HADDLVAVSA KQAKQV 

« Hide

References

[1]"Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, a non-pathogenic variant closely related to the well-characterized pathogenic strain H37Rv."
Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25177 / H37Ra.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000611 Genomic DNA. Translation: ABQ74235.1.
RefSeqYP_001283797.1. NC_009525.1.

3D structure databases

ProteinModelPortalA5U5D5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5U5D5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000066736; EBMYCP00000064846; EBMYCG00000066731.
GeneID5212869.
GenomeReviewsGene locus MRA_2465 in contig CP000611_GR.
KEGGmra:MRA_2465.
PATRIC18145152. VBIMycTub106795_2774.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
GeneTreeEBGT00050000017499.
HOGENOMHBG507643.
OMATFGDNDM.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycMTUB419947:MRA_2465-MONOMER.

Family and domain databases

HAMAPMF_00456. ProB.
[Tree]
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]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
KOK00931.
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF53633. Aa_kinase. 1 hit.
SSF88697. PUA-like. 1 hit.
TIGRFAMsTIGR01027. ProB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_MYCTA
AccessionPrimary (citable) accession number: A5U5D5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families