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Q735X2

- PROB_BACC1

UniProt

Q735X2 - PROB_BACC1

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Protein

Glutamate 5-kinase

Gene

proB

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate.UniRule annotation

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei9 – 91ATPUniRule annotation
Binding sitei49 – 491SubstrateUniRule annotation
Binding sitei136 – 1361SubstrateUniRule annotation
Binding sitei148 – 1481Substrate; via amide nitrogenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi168 – 1692ATPUniRule annotation
Nucleotide bindingi210 – 2167ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate 5-kinase activity Source: UniProtKB-HAMAP
  3. RNA binding Source: InterPro

GO - Biological processi

  1. L-proline biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00098; UER00359.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate 5-kinaseUniRule annotation (EC:2.7.2.11UniRule annotation)
Alternative name(s):
Gamma-glutamyl kinaseUniRule annotation
Short name:
GKUniRule annotation
Gene namesi
Name:proBUniRule annotation
Ordered Locus Names:BCE_3029
OrganismiBacillus cereus (strain ATCC 10987)
Taxonomic identifieri222523 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
ProteomesiUP000002527: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Glutamate 5-kinasePRO_0000109633Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi222523.BCE_3029.

Structurei

3D structure databases

ProteinModelPortaliQ735X2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini276 – 35075PUAUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutamate 5-kinase family.UniRule annotation
Contains 1 PUA domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0263.
HOGENOMiHOG000246368.
KOiK00931.
OMAiHRLEVIH.
OrthoDBiEOG6PGK7G.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB.
InterProiIPR001048. 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]
PfamiPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFiPIRSF000729. GK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q735X2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKQRIVVKI GSSSLADSHG GISKEQLSDH VAALARLKEE GHEVLLITSG
60 70 80 90 100
AVAAGFSALG YPSRPVTIKG KQAAAAVGQS LLMQAYTEEF RKYGIVTAQL
110 120 130 140 150
LLTRSDFSRK EQYSNAYATL GELLNRSALP IINENDSISL EELTFGDNDM
160 170 180 190 200
LSALVSGLVS ADMLMIFTDV NGLYDKNPQK NEDAKKYYFL PEVTEEIASL
210 220 230 240 250
AGDAGSKLGT GGMKSKIDAA KTALSLGVSV FIGTGRGQEK FVDVLKGKGD
260 270 280 290 300
GTYVGNAPQK EIKMNKQWIA LHSVVSGQIE IDAGAATAII QHGKSLLPAG
310 320 330 340 350
VTNVSGFFKV GDVVEVMTQQ GRVIGKGQCT YSAEELREIK GMQSQHIQAR
360
GERHNYEVIH RDHWVSL
Length:367
Mass (Da):39,505
Last modified:July 5, 2004 - v1
Checksum:i4CF37DBBD80B0D3F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS41940.1.
RefSeqiNP_979332.1. NC_003909.8.
WP_000744720.1. NC_003909.8.

Genome annotation databases

EnsemblBacteriaiAAS41940; AAS41940; BCE_3029.
GeneIDi2747545.
KEGGibca:BCE_3029.
PATRICi18854792. VBIBacCer118379_2896.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017194 Genomic DNA. Translation: AAS41940.1 .
RefSeqi NP_979332.1. NC_003909.8.
WP_000744720.1. NC_003909.8.

3D structure databases

ProteinModelPortali Q735X2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 222523.BCE_3029.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAS41940 ; AAS41940 ; BCE_3029 .
GeneIDi 2747545.
KEGGi bca:BCE_3029.
PATRICi 18854792. VBIBacCer118379_2896.

Phylogenomic databases

eggNOGi COG0263.
HOGENOMi HOG000246368.
KOi K00931.
OMAi HRLEVIH.
OrthoDBi EOG6PGK7G.

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00359 .

Family and domain databases

Gene3Di 2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPi MF_00456. ProB.
InterProi IPR001048. 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 ]
Pfami PF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view ]
PIRSFi PIRSF000729. GK. 1 hit.
PRINTSi PR00474. GLU5KINASE.
SMARTi SM00359. PUA. 1 hit.
[Graphical view ]
SUPFAMi SSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR01027. proB. 1 hit.
PROSITEi PS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
    Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
    Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 10987.

Entry informationi

Entry nameiPROB_BACC1
AccessioniPrimary (citable) accession number: Q735X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3