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Q81P26 (PROB_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. 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:BA_2993, GBAA_2993, BAS2782
OrganismBacillus anthracis
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

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. 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 HAMAP MF_00456.

Sequence similarities

Belongs to the glutamate 5-kinase family.

Contains 1 PUA domain.

Sequence caution

The sequence AAT55091.1 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
Reference proteome
Gene Ontology (GO)
   Biological processproline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Glutamate 5-kinase HAMAP MF_00456
PRO_0000109632

Regions

Domain276 – 35075PUA

Sequences

Sequence LengthMass (Da)Tools
Q81P26 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 259620BA1F3975AD

FASTA36739,600
        10         20         30         40         50         60 
MKKQRIVVKI GSSSLADSHE GISKEQLSDH VAALARLKEE GHEVLLITSG AVAAGFSALG 

        70         80         90        100        110        120 
YPSRPVTIKG KQAAAAVGQS LLMQAYTEEF RKYGIVTAQL LLTRSDFSRK EQYSNAYATL 

       130        140        150        160        170        180 
GELLNRSALP IINENDSISL EELTFGDNDM LSALVSGLVS ADMLMIFTDV NGLYDKNPQK 

       190        200        210        220        230        240 
NEDAKKYYFL PEVTEEIASL AGDAGSKLGT GGMKSKVDAA KTALSLGVSV FIGTGRGQEK 

       250        260        270        280        290        300 
FVDVLKGKGD GTYVGNAPQK EMKINKQWIA LHSVVSGQIE IDAGAATAII QHGKSLLPAG 

       310        320        330        340        350        360 
VTNVSGFFQV GEVVEVMTQQ GRVIGKGQCT YSAEELRDVK GMQSQQIQAR GERHNYEVIH 


RDYWVSF 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP26812.1.
AE017334 Genomic DNA. Translation: AAT32111.2.
AE017225 Genomic DNA. Translation: AAT55091.1. Different initiation.
RefSeqNP_845326.1. NC_003997.3.
YP_019636.2. NC_007530.2.

3D structure databases

ProteinModelPortalQ81P26.
ModBaseSearch...

Protein-protein interaction databases

IntActQ81P26. 3 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000012665; EBBACP00000012421; EBBACG00000012657.
EBBACT00000014997; EBBACP00000014618; EBBACG00000014989.
EBBACT00000024286; EBBACP00000023771; EBBACG00000024277.
GeneID1086339.
2819367.
GenomeReviewsGene locus BA_2993 in contig AE016879_GR.
Gene locus BAS2782 in contig AE017225_GR.
Gene locus GBAA_2993 in contig AE017334_GR.
KEGGban:BA_2993.
bar:GBAA_2993.
bat:BAS2782.
PATRIC18783598. VBIBacAnt69550_2974.
TIGRBA_2993.
GBAA_2993.

Phylogenomic databases

GeneTreeEBGT00050000001887.
HOGENOMHBG507643.
OMATFGDNDM.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycBANT260799:BAS2782-MONOMER.
BANT261594:GBAA2993-MONOMER.

Family and domain databases

HAMAPMF_00456. ProB.
[Tree]
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]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
KOK00931.
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF53633. Aa_kinase. 1 hit.
SSF88697. PUA-like. 1 hit.
TIGRFAMsTIGR01027. ProB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_BACAN
AccessionPrimary (citable) accession number: Q81P26
Secondary accession number(s): Q6HX98, Q6KRC0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2003
Last modified: January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families