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A2SD37

- PROB_METPP

UniProt

A2SD37 - PROB_METPP

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Protein

Glutamate 5-kinase

Gene

proB

Organism
Methylibium petroleiphilum (strain PM1)
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 sitei14 – 141ATPUniRule annotation
Binding sitei54 – 541SubstrateUniRule annotation
Binding sitei141 – 1411SubstrateUniRule annotation
Binding sitei153 – 1531Substrate; via amide nitrogenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1742ATPUniRule 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

BioCyciMPET420662:GHBE-521-MONOMER.
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:Mpe_A0514
OrganismiMethylibium petroleiphilum (strain PM1)
Taxonomic identifieri420662 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
ProteomesiUP000000366: 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 – 372372Glutamate 5-kinasePRO_1000081071Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi420662.Mpe_A0514.

Structurei

3D structure databases

ProteinModelPortaliA2SD37.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 35879PUAUniRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0263.
HOGENOMiHOG000246368.
KOiK00931.
OMAiMRMIAGH.
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.

A2SD37-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEVLRGARR IVVKVGSSLV TNEGRGVDAA AIGNWCRQLA SLAGQGREVL
60 70 80 90 100
MVSSGAIAEG MKRLGWNARP KEIHELQAAA AVGQMGLAQM YESKLSEHGI
110 120 130 140 150
GSAQVLLTHA DLADRERYLN ARSTLLTLLS LKVIPVINEN DTVVNDEIKF
160 170 180 190 200
GDNDTLGALV ANLVDADALV ILTDQPGLYS ADPRKDPQAR FIGEAVAGTP
210 220 230 240 250
ELERMAGGAG SSLGRGGMIT KVLAAKRASS SGASTVIAWG REPDVLLRLA
260 270 280 290 300
DGEAIGTLLV ARTAKLAARK QWMADHLQMR GTVVIDDGAV AKLRDEGKSL
310 320 330 340 350
LPIGVVEVQG EFVRGDVIAV RSQVGIEIAR GLANYASSEA RLIARKPSSQ
360 370
IESLLGYSNE PEMIHRTNLV LA
Length:372
Mass (Da):39,424
Last modified:March 6, 2007 - v1
Checksum:iC70575C68FB44FFE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000555 Genomic DNA. Translation: ABM93476.1.
RefSeqiYP_001019711.1. NC_008825.1.

Genome annotation databases

EnsemblBacteriaiABM93476; ABM93476; Mpe_A0514.
GeneIDi4787090.
KEGGimpt:Mpe_A0514.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000555 Genomic DNA. Translation: ABM93476.1 .
RefSeqi YP_001019711.1. NC_008825.1.

3D structure databases

ProteinModelPortali A2SD37.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 420662.Mpe_A0514.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABM93476 ; ABM93476 ; Mpe_A0514 .
GeneIDi 4787090.
KEGGi mpt:Mpe_A0514.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00359 .
BioCyci MPET420662:GHBE-521-MONOMER.

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. "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
    Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
    J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PM1.

Entry informationi

Entry nameiPROB_METPP
AccessioniPrimary (citable) accession number: A2SD37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 6, 2007
Last modified: October 29, 2014
This is version 55 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, Reference proteome

Documents

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

External Data

Dasty 3