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Q21M06 (PROB_SACD2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:Sde_1011
OrganismSaccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024) [Complete proteome] [HAMAP]
Taxonomic identifier203122 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeSaccharophagus

Protein attributes

Sequence length373 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 – 373373Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000252999

Regions

Domain281 – 35979PUA
Nucleotide binding175 – 1762ATP By similarity

Sites

Binding site161ATP By similarity
Binding site561Substrate By similarity
Binding site1431Substrate By similarity
Binding site1551Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q21M06 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 4B3FF3EA2B5355BC

FASTA37340,627
        10         20         30         40         50         60 
MSKRQLVKQS RRWVIKIGSA LLTNNGRGLD REEMAVWVKQ MAALSKRGYE VVLVSSGAVA 

        70         80         90        100        110        120 
AGMTRLGWAE RPKALHELQA AAAVGQSSLI QAYEQEFQKY SIKTAQILLD HDDLSNRQRY 

       130        140        150        160        170        180 
LNARSTLRTL TKLGVIPIVN ENDTVVTDEI RFGDNDTLGA LVANLIEADT LCILTDQKAM 

       190        200        210        220        230        240 
FDSDPRQNAL AKMLIERSAF DPGLDAMAGD GGALGRGGMI SKVRAARLAA RSGANTIVVG 

       250        260        270        280        290        300 
GKVFDVIPRV ASGEILGTLL YSESQPIAAR KRWLAGNMQP RGRLTLDDGA VKVLREQGKS 

       310        320        330        340        350        360 
LLPVGVRAVE GYFTRGELVL CEDTAGREIA RGLVNYSSDE TNKIKGASSS RIDSLLGYKD 

       370 
YDELIHRDNL VLV 

« Hide

References

[1]"Complete genome sequence of the complex carbohydrate-degrading marine bacterium, Saccharophagus degradans strain 2-40 T."
Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M., Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H., Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R., Richardson P.M., Borovok I., Hutcheson S.
PLoS Genet. 4:E1000087-E1000087(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2-40 / ATCC 43961 / DSM 17024.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000282 Genomic DNA. Translation: ABD80273.1.
RefSeqYP_526485.1. NC_007912.1.

3D structure databases

ProteinModelPortalQ21M06.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203122.Sde_1011.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD80273; ABD80273; Sde_1011.
GeneID3965136.
KEGGsde:Sde_1011.
PATRIC23400815. VBISacDeg56404_1106.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMARLMRAYE.
OrthoDBEOG6PGK7G.

Enzyme and pathway databases

BioCycSDEG203122:GI2M-1022-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_SACD2
AccessionPrimary (citable) accession number: Q21M06
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: April 18, 2006
Last modified: May 14, 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