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Q6A9H7 (PROB_PROAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:PPA0834
OrganismPropionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]
Taxonomic identifier267747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length391 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.

Sequence caution

The sequence AAT82589.1 differs from that shown. Reason: Erroneous initiation.

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 – 391391Glutamate 5-kinase HAMAP-Rule MF_00456
PRO_0000109705

Regions

Domain278 – 35679PUA
Nucleotide binding176 – 1772ATP By similarity
Nucleotide binding216 – 2227ATP 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
Q6A9H7 [UniParc].

Last modified September 13, 2005. Version 2.
Checksum: 0055C23FF1493E22

FASTA39140,984
        10         20         30         40         50         60 
MTDQRGAICG AATLVVKVGS SSLTLPGGGI DVRRVDDLVD ALSEVIAVGR RVVLVSSGAI 

        70         80         90        100        110        120 
ATGFPAMGIT HRPRTLAGKQ AAASVGQGIL LAHYASRFAS HGLRVGQVLL TVNDLVRPTS 

       130        140        150        160        170        180 
YRNAWSTLDT LLGLGVVPIV NENDTVATGE IRFGDNDRLA ALVAELVRAQ ALILLSDVDA 

       190        200        210        220        230        240 
LYTAHPDSPD ARRVEVVEDI DTLDVDTHKA GSGVGTGGMT TKLEAARMAT CAGVPVVLAA 

       250        260        270        280        290        300 
AVDAPDVLAG VPVGTYFRPL ATRRPRRLLW LADAATPQGQ IVIDDGAVEA LTQRHSSLLA 

       310        320        330        340        350        360 
VGVTRVHGDF QAGDPVTILA SDGRVVGRGI AQFSHDEVRV MRGRSSAWLA AEMGPAASRE 

       370        380        390 
IIHRDAMVLS RRRKAEPSSR NQKSSGSRVT S 

« Hide

References

[1]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017283 Genomic DNA. Translation: AAT82589.1. Different initiation.
RefSeqYP_055547.1. NC_006085.1.

3D structure databases

ProteinModelPortalQ6A9H7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING267747.PPA0834.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT82589; AAT82589; PPA0834.
GeneID2932500.
KEGGpac:PPA0834.
PATRIC23036387. VBIProAcn64440_0869.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246368.
KOK00931.
OMAPPTIASK.
OrthoDBEOG6PGK7G.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycPACN267747:GHO9-843-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_PROAC
AccessionPrimary (citable) accession number: Q6A9H7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 65 of the entry and version 2 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