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P71910 (PROB_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. 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:Rv2439c, MT2515
ORF Names:MTCY428.07
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [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. 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.

Miscellaneous

Was identified as a high-confidence drug target. 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
Reference proteome
Gene Ontology (GO)
   Biological processgrowth

Inferred from mutant phenotype. Source: MTBBASE

proline 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_0000109696

Regions

Domain280 – 35879PUA

Experimental info

Sequence conflict2261A → S in AAK46812. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P71910 [UniParc].

Last modified February 1, 1997. 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]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842579 Genomic DNA. Translation: CAB03780.1.
AE000516 Genomic DNA. Translation: AAK46812.1.
PIRE70680.
RefSeqNP_216955.1. NC_000962.2.
NP_336998.1. NC_002755.2.

3D structure databases

ProteinModelPortalP71910.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000003064; EBMYCP00000003064; EBMYCG00000003062.
EBMYCT00000070118; EBMYCP00000068177; EBMYCG00000070113.
GeneID885266.
925792.
GenomeReviewsGene locus MT2515 in contig AE000516_GR.
Gene locus Rv2439c in contig AL123456_GR.
KEGGmtc:MT2515.
mtu:Rv2439c.
PATRIC18127280. VBIMycTub22151_2748.
TIGRMT2515.

Organism-specific databases

TubercuListRv2439c.

Phylogenomic databases

GeneTreeEBGT00050000017499.
HOGENOMHBG507643.
OMATFGDNDM.
PhylomeDBP71910.
ProtClustDBPRK05429.

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_MYCTU
AccessionPrimary (citable) accession number: P71910
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 83 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