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P0C1E3

- PROB_CORML

UniProt

P0C1E3 - PROB_CORML

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Protein
Glutamate 5-kinase
Gene
proB
Organism
Corynebacterium melassecola
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 By similarity.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141ATP By similarity
Binding sitei56 – 561Substrate By similarity
Binding sitei143 – 1431Substrate By similarity
Binding sitei155 – 1551Substrate; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi175 – 1762ATP By similarity
Nucleotide bindingi215 – 2217ATP By similarity

GO - Molecular functioni

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

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-kinase (EC:2.7.2.11)
Alternative name(s):
Gamma-glutamyl kinase
Short name:
GK
Gene namesi
Name:proB
OrganismiCorynebacterium melassecola
Taxonomic identifieri41643 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 369369Glutamate 5-kinaseUniRule annotation
PRO_0000236037Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP0C1E3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini277 – 35175PUA
Add
BLAST

Sequence similaritiesi

Contains 1 PUA domain.

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.

P0C1E3-1 [UniParc]FASTAAdd to Basket

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MRERISNAKR VVVKIGSSSL TNDEDGHTVD PNRINTIVNA LQARMEAGSD    50
LIVVSSGAVA AGMAPLGLST RPTELAVKQA AAAVGQVHLM HQWGRSFARY 100
GRPIGQVLLT AADAGKRDRA RNAQRTIDKL RILGAVPIVN ENDTVATTGV 150
NFGDNDRLAA IVAHLVSADA LVLLSDVDGL FDKNPTDPTA KFISEVRDGN 200
DLKGVIAGDG GKVGTGGMAS KVSAARLASR SGVPVLLTSA ANIGPALEDA 250
QVGTVFHPKD NRLSAWKFWA LYAADTAGKI RLDDGAVEAV TSGGKSLLAV 300
GITEIIGDFQ QGEIVEILGP AGQIIGRGEV SYDSDTLQSM VGMQTQDLPD 350
GMQRPVVHAD YLSNYASRA 369
Length:369
Mass (Da):38,626
Last modified:May 16, 2006 - v1
Checksum:iE7CC949DBBDFC77F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31230 Genomic DNA. Translation: AAC44174.1.
PIRiT50666.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U31230 Genomic DNA. Translation: AAC44174.1 .
PIRi T50666.

3D structure databases

ProteinModelPortali P0C1E3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Mutations in the Corynebacterium glutamicum proline biosynthetic pathway: a natural bypass of the proA step."
    Ankri S., Serebrijski I., Reyes O., Leblon G.
    J. Bacteriol. 178:4412-4419(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 17965 / AS B-4821.

Entry informationi

Entry nameiPROB_CORML
AccessioniPrimary (citable) accession number: P0C1E3
Secondary accession number(s): P46546
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: September 3, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

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

External Data

Dasty 3

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