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A0R148 (PROB_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 44. 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:MSMEG_4621
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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
Reference 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

Initiator methionine11Removed Ref.2
Chain2 – 370369Glutamate 5-kinase HAMAP MF_00456
PRO_1000081076

Regions

Domain282 – 36079PUA

Sequences

Sequence LengthMass (Da)Tools
A0R148 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 878693E7975F7CFB

FASTA37038,607
        10         20         30         40         50         60 
MSEHREAVRT ARSVVVKIGT TALTTPSGVF DANRLASLVE AIEGRMKAGS DVVIVSSGAI 

        70         80         90        100        110        120 
AAGIEPLGLS KRPTDLATKQ AAASVGQVAL VNAWSAAFAV YNRTVGQVLL TAHDISMRVQ 

       130        140        150        160        170        180 
HNNAQRTLDR LRALHAVAIV NENDTVATNE IRFGDNDRLS ALVAHLVGAD ALILLSDIDG 

       190        200        210        220        230        240 
LYDGDPRKAT PDKPARFIPE VAAQGDLDGV VAGRGSSLGT GGMASKLSSA LLAADAGVPV 

       250        260        270        280        290        300 
LLAAAADAGR ALDDASVGTV FAPRPERMSA RKFWMRYAAE SAGALTLDDG AVRAVIKQRR 

       310        320        330        340        350        360 
SLLPAGITSV TGRFHGGDVV DLRALDGHTV ARGVVAYDQA ELASIIGRST HELPVEMRRP 

       370 
AVHADDLVRT 

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed: 18955433] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000480 Genomic DNA. Translation: ABK71775.1.
RefSeqYP_888886.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0R148.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0R148.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000043693; EBMYCP00000042030; EBMYCG00000043688.
GeneID4531097.
GenomeReviewsGene locus MSMEG_4621 in contig CP000480_GR.
KEGGmsm:MSMEG_4621.
NMPDRfig|246196.1.peg.4614.
PATRIC18081557. VBIMycSme59918_4517.
TIGRMSMEG_4621.

Phylogenomic databases

eggNOGCOG0263.
GeneTreeEBGT00050000017499.
HOGENOMHBG507643.
OMATFGDNDM.
PhylomeDBA0R148.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycMSME246196:MSMEG_4621-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_MYCS2
AccessionPrimary (citable) accession number: A0R148
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 44 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