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Reviewed, UniProtKB/Swiss-Prot Q3IHK8 (PROB2_PSEHT)

Last modified November 3, 2009. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Glutamate 5-kinase 2
    EC=2.7.2.11
Alternative name(s):
    Gamma-glutamyl kinase 2
      Short name=GK 2
Gene names
Name: proB2
Ordered Locus Names: PSHAa0633
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. 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.

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 processproline biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Glutamate 5-kinase 2 HAMAP MF_00456
PRO_0000230056

Regions

Domain275 – 35379PUA

Sequences

Sequence LengthMass (Da)Tools
Q3IHK8-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: CE911995481AF222

FASTA36739,084
        10         20         30         40         50         60 
MQRDQVIVVK LGTSVLTGGT DKLDKAHMVE LVRQCCELKK QGHHVILVSS GAVAAGREQL 

        70         80         90        100        110        120 
LKPCGRSVID KQMLAAVGQG QLIHIWQSLF ALYGVNVGQM LLTRADVNDR ERYLNARDTL 

       130        140        150        160        170        180 
NALLNYDVVP IINENDAVAT SEIKVGDNDN LSALVAILAN ANKLLLLTDQ EGLFTSDPRT 

       190        200        210        220        230        240 
NADATLIGEV SDINDELRQL AGGSGTNLGT GGMATKLQAA DIARRAGVEV IIAKGAGKNV 

       250        260        270        280        290        300 
ILKCMSEQLP GTRFLKLTAP KEGRKKWLLA GPKSSGQIVI DAGAITALQT KGASLLAKGV 

       310        320        330        340        350        360 
TNALGAFERG DLISVINSDK QLIARGLTRF SSSEVNKIKG AHSKQIGELL DYDGGAEVLH 


RDDLILL 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR954246 Genomic DNA. Translation: CAI85718.1.
RefSeqYP_339161.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IHK8.

Genome annotation databases

GeneID3709848.
GenomeReviewsGene locus PSHAa0633 in contig CR954246_GR.
KEGGpha:PSHAa0633.
NMPDRfig|326442.4.peg.604.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ3IHK8.
OMAILTDQRG.

Enzyme and pathway databases

BioCycPHAL326442:PSHAA0633-MON.

Family and domain databases

HAMAPMF_00456.
[Tree]
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu_5kinase.
IPR011529. Glu_5kinase_bact.
IPR019797. Glutamate_5-kinase_CS.
IPR005715. ProB.
IPR002478. PUA.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB2_PSEHT
AccessionPrimary (citable) accession number: Q3IHK8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: November 3, 2009
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents