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Q5WVX6

- GLND_LEGPL

UniProt

Q5WVX6 - GLND_LEGPL

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, lpl1684
Organism
Legionella pneumophila (strain Lens)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism By similarity.UniRule annotation

Catalytic activityi

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity.UniRule annotation

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. metal ion binding Source: InterPro
  4. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. nitrogen compound metabolic process Source: InterPro
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciLPNE297245:GJD4-1810-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Short name:
UTase/UR
Alternative name(s):
Bifunctional [protein-PII] modification enzyme
Bifunctional nitrogen sensor protein
Including the following 2 domains:
[Protein-PII] uridylyltransferase (EC:2.7.7.59)
Short name:
PII uridylyltransferase
Short name:
UTase
[Protein-PII]-UMP uridylyl-removing enzyme (EC:3.1.4.-)
Short name:
UR
Gene namesi
Name:glnD
Ordered Locus Names:lpl1684
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
ProteomesiUP000002517: Chromosome

Organism-specific databases

LegioListilpl1684.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 861861Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_0000192740Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi297245.lpl1684.

Structurei

3D structure databases

ProteinModelPortaliQ5WVX6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini441 – 569129HDAdd
BLAST
Domaini679 – 76082ACT 1Add
BLAST
Domaini788 – 86174ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 321321UridylyltransferaseUniRule annotationAdd
BLAST
Regioni322 – 678357Uridylyl-removingUniRule annotationAdd
BLAST

Domaini

Has four distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, a central HD domain that encodes UR activity, and two C-terminal ACT domains that seem to have a role in glutamine sensing By similarity.UniRule annotation

Sequence similaritiesi

Belongs to the GlnD family.
Contains 2 ACT domains.
Contains 1 HD domain.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiHHLLMSV.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR005105. GlnD_Uridyltrans_N.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF03445. DUF294. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
[Graphical view]
PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5WVX6-1 [UniParc]FASTAAdd to Basket

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MKNDNRIIKN TIKQFKEKLC RDFSQKANIT SITRKLAVFI DTILIQLFIK    50
NKLHFGDNFC LLALGSYGRR ELQLHSDIDL LILHTEKVSN IQLQRAQKFI 100
QDCWDVGLEV SHQITTVSSC ANLASQDLSV ISTIMDMFLL CGHGALMEEL 150
IYQTHTLHMW PSHQYFFAKL QEQQSRYAKY GETAYNLEPN IKNGPGGLRD 200
LQILLSISKR HFKIKKLAEG IGYGFITDKE YEELKYCQNF LWRVRFALHM 250
LAGKPEERLS FDYQVKLAQF FGYQDQSHIL AIEQFMKDYF KVIKRNRELN 300
EMLLQWFNET IVYHQKQKII RLDDEFQLSN RFIEVRNNRV FKQNPQSILK 350
LFYWLVKRPD IEGVRASTIR LIRESLFLMG KRFRESKETA NIFVNIFRTG 400
NDPYDALQRM NRYGVLAHYL DCFATVTGQM QYDLFHAYTV DQHTLFVIRN 450
ISRFKKNEYA KQFPLCAKII TALEKPEILY LGALFHDIAK GRGGDHSELG 500
AIEAQQFTQR HYMEAEDSKL IVWLVRYHLL MSQTAQRKDI YDPKTIEQFC 550
QLLPHAKYLD YLYLLTVADI CGTNPTLWNA WKDSLLKELY HAAKTRLHKQ 600
QELLDEAALI SIRKQYAMDI LISDGISSRV IQDLWSQFKG KYFLHESPEV 650
IARHTKAILN SKQFPVVIIM PHHSQGGTEV FIYMPHKDER FTITTSVLSN 700
HHVTIQEAAI ITCDNQFDLD TYIILDENNQ AFLNEQRARD IQKSLCDHLA 750
NTGRLPAVSR RRLSRALTHF NVKTQINFID DNTNHQTQLF LVTNDRPGLL 800
ATISRVFLTL NIHLHNAKIA TAGERVEDMF YISNQTGYSL NHEEKTILKE 850
KLILEISKSK Y 861
Length:861
Mass (Da):100,671
Last modified:November 23, 2004 - v1
Checksum:i4D1AB5D391DCE105
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH15924.1.
RefSeqiYP_127023.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH15924; CAH15924; lpl1684.
GeneIDi3113365.
KEGGilpf:lpl1684.
PATRICi22317079. VBILegPne33733_1866.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR628337 Genomic DNA. Translation: CAH15924.1 .
RefSeqi YP_127023.1. NC_006369.1.

3D structure databases

ProteinModelPortali Q5WVX6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 297245.lpl1684.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAH15924 ; CAH15924 ; lpl1684 .
GeneIDi 3113365.
KEGGi lpf:lpl1684.
PATRICi 22317079. VBILegPne33733_1866.

Organism-specific databases

LegioListi lpl1684.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci LPNE297245:GJD4-1810-MONOMER.

Family and domain databases

Gene3Di 1.10.3210.10. 1 hit.
HAMAPi MF_00277. PII_uridylyl_transf.
InterProi IPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR005105. GlnD_Uridyltrans_N.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF03445. DUF294. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
[Graphical view ]
PIRSFi PIRSF006288. PII_uridyltransf. 1 hit.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01693. UTase_glnD. 1 hit.
PROSITEi PS51671. ACT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
    Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
    Nat. Genet. 36:1165-1173(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lens.

Entry informationi

Entry nameiGLND_LEGPL
AccessioniPrimary (citable) accession number: Q5WVX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 23, 2004
Last modified: June 11, 2014
This is version 65 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, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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