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Q2LR78 (PROB_SYNAS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:SYNAS_07070
ORF Names:SYN_01350
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus

Protein attributes

Sequence length385 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 – 385385Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000253013

Regions

Domain283 – 36179PUA
Nucleotide binding218 – 2247ATP By similarity

Sites

Binding site181ATP By similarity
Binding site571Substrate By similarity
Binding site1441Substrate By similarity
Binding site1561Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LR78 [UniParc].

Last modified February 21, 2006. Version 1.
Checksum: EB7693F3FB5B0167

FASTA38542,139
        10         20         30         40         50         60 
MNENREQVLK NVKRVLIKIG SAVLTGDNGL DLERIQHLVD QMAALTHRGY QVVMVTSGAI 

        70         80         90        100        110        120 
ASGKHRLGIT TALKSIPQKQ AAAAIGQGRL MRIYSNSFGK HGLYVGQILL TMSDLTDRRR 

       130        140        150        160        170        180 
FLNIRNTLST LMEWGIIAII NENDTVAIDE IKFGDNDNLA AMIANIIEAH LVINLTSTPG 

       190        200        210        220        230        240 
LYDRNPASSR NARLIPLVRE ITEDIEAAAS EEGTSVGTGG MKSKVMAAKK VTAFGIPYII 

       250        260        270        280        290        300 
APGKQKDVLL DIFDGNELGT LFLPMREHLS SRKYWIAFTL RSRGVLSIDA GARTAILEEG 

       310        320        330        340        350        360 
KSLLPSGIVG VEGDFIVGDP VTCVDRDGVP LAKGLVNYSA PDIRKIMGLK TSRIEQVLGH 

       370        380 
KDYDEIIHRD NLAVIRRSRR HREAG 

« Hide

References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000252 Genomic DNA. Translation: ABC76586.1.
RefSeqYP_460754.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LR78.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING56780.SYN_01350.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC76586; ABC76586; SYN_01350.
GeneID3884768.
KEGGsat:SYN_01350.
PATRIC23861905. VBISynAci70500_0769.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMATVIHRDN.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycSACI56780:GHXT-722-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_SYNAS
AccessionPrimary (citable) accession number: Q2LR78
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: February 21, 2006
Last modified: February 19, 2014
This is version 58 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