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Q73XP6 (PROB_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 72. 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:MAP_2263c
OrganismMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]
Taxonomic identifier262316 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length367 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 – 367367Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109695

Regions

Domain279 – 35779PUA
Nucleotide binding176 – 1772ATP By similarity
Nucleotide binding217 – 2237ATP By similarity

Sites

Binding site171ATP By similarity
Binding site571Substrate By similarity
Binding site1441Substrate By similarity
Binding site1561Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73XP6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 734647E2226C9426

FASTA36737,889
        10         20         30         40         50         60 
MTAHRDAIRT ARSMVVKVGT NALTTPAGVF DAGRLAGLAD AIEARMKAGT DVVIVSSGAI 

        70         80         90        100        110        120 
AAGIEPLGLS RRPRDLATKQ AAASVGQVAL VNSWSAAFAR YGRTVGQVLL SAHDISMRAQ 

       130        140        150        160        170        180 
HTNAQRTLDR LRALHAVAIV NENDTVATNE IRFGDNDRLS ALVAHLVGAE ALVLLSDIDG 

       190        200        210        220        230        240 
LYDSDPRKTK GAKFIPEVTG AEDLAGVVAG PGSDLGTGGM TSKMSSALLA ADAGVPVLLA 

       250        260        270        280        290        300 
AAADAASALT DASVGTVFAA RPVRMSARRF WVRYAAEAAG ALTLDEGAVR AVVHQRRSLL 

       310        320        330        340        350        360 
PAGITAVSGR FYAGDVVELR GPDAVPVARG VVAYDTTELA TMMGRSTSEL PGELRRPAVH 


ADDLVAV 

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS04580.1.
RefSeqNP_961197.1. NC_002944.2.

3D structure databases

ProteinModelPortalQ73XP6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262316.MAP2263c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS04580; AAS04580; MAP_2263c.
GeneID2718537.
KEGGmpa:MAP2263c.
PATRIC17997164. VBIMycAvi108102_2406.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
KOK00931.
OMAFDAKEIP.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycMAVI262316:GCQR-2289-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_MYCPA
AccessionPrimary (citable) accession number: Q73XP6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 72 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