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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Legionella pneumophila (strain Paris)
Status
Reviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciLPNE297246:GCO9-2171-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
Short name:
UTase/URUniRule annotation
Alternative name(s):
Bifunctional [protein-PII] modification enzymeUniRule annotation
Bifunctional nitrogen sensor proteinUniRule annotation
Including the following 2 domains:
[Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
Short name:
PII uridylyltransferaseUniRule annotation
Short name:
UTaseUniRule annotation
[Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
Short name:
URUniRule annotation
Gene namesi
Name:glnDUniRule annotation
Ordered Locus Names:lpp1685
OrganismiLegionella pneumophila (strain Paris)
Taxonomic identifieri297246 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Organism-specific databases

LegioListilpp1685.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 861861Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192741Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi297246.lpp1685.

Structurei

3D structure databases

ProteinModelPortaliQ5X4J1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini441 – 570130HDUniRule annotationAdd
BLAST
Domaini679 – 76082ACT 1UniRule annotationAdd
BLAST
Domaini788 – 86174ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 321321UridylyltransferaseAdd
BLAST
Regioni322 – 678357Uridylyl-removingAdd
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.UniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiCFATVTG.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR005105. GlnD_Uridyltrans_N.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[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.

Q5X4J1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNDNRIIKN TIKQFKEKLC KDFSQKANIT SITRKLAVFI DTILIQLFIK
60 70 80 90 100
NKLHFGDNFC LLALGSYGRR ELQLHSDIDL LILHTEKVSN IQLQRAQKFI
110 120 130 140 150
QDCWDVGLEV SHQITTVSSC ANLASQDLSV ISTIMDMFLL CGHGALMEEL
160 170 180 190 200
IYQTHTLHMW PSHQYFFAKL QEQQNRYAKY GETAYNLEPN IKNGPGGLRD
210 220 230 240 250
LQILLSISKR HFKIKKLAEG IGYGFITDKE YEELKYCQNF LWRVRFALHM
260 270 280 290 300
LAGKPEERLS FDYQVKLAQF FGYQDQSHIL AIEQFMKDYF KVIKRNRELN
310 320 330 340 350
EMLLQWFNET IVYHQKQKII RLDDEFQLSN RFIEVRNNRV FKQNPQSILK
360 370 380 390 400
LFYWLVKRPD IEGVRASTIR LIRESLFLMG KRFRESKETA NIFINIFRTG
410 420 430 440 450
NDPYDALQRM NRYGVLAHYL DCFATVTGQM QYDLFHAYTV DQHTLFVIRN
460 470 480 490 500
ISRFKKNEYA KQFPLCAKII SALEKPEILY LGALFHDIAK GRGGDHSELG
510 520 530 540 550
AIEAQQFTQR HYMEAEDSKL IVWLVRYHLL MSQTAQRKDI YDPKTIEQFC
560 570 580 590 600
QLLPHARYLD YLYLLTVADI CGTNPTLWNA WKDSLLKELY HAAKTRLHKQ
610 620 630 640 650
QELLDEAALI SIRKQYAMDI LISDGISSRV IQDLWSQFKG KYFLHESPEV
660 670 680 690 700
IARHTKAILN SKQFPVVIIM PHHSQGGTEV FIYMPHKDER FTITTSVLSN
710 720 730 740 750
HHVTIQEAAI ITCDNQFDLD TYIILDENNQ AFLNEQRARD IQKSLCDHLA
760 770 780 790 800
NTGRLPAVSR RRLSRALTHF NVKTQINFID DNTNHQTQLF LVTNDRPGLL
810 820 830 840 850
ATISRVFLTL NIHLHNAKIA TAGERVEDMF YISNQTGYSL NHEEKTILKE
860
KLILEISKSK Y
Length:861
Mass (Da):100,698
Last modified:November 23, 2004 - v1
Checksum:iD649CBF8276315C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628336 Genomic DNA. Translation: CAH12837.1.
RefSeqiWP_011213990.1. NC_006368.1.
YP_124003.1. NC_006368.1.

Genome annotation databases

EnsemblBacteriaiCAH12837; CAH12837; lpp1685.
KEGGilpp:lpp1685.
PATRICi22323790. VBILegPne27771_1951.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628336 Genomic DNA. Translation: CAH12837.1.
RefSeqiWP_011213990.1. NC_006368.1.
YP_124003.1. NC_006368.1.

3D structure databases

ProteinModelPortaliQ5X4J1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi297246.lpp1685.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH12837; CAH12837; lpp1685.
KEGGilpp:lpp1685.
PATRICi22323790. VBILegPne27771_1951.

Organism-specific databases

LegioListilpp1685.

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiCFATVTG.
OrthoDBiEOG6CCH44.

Enzyme and pathway databases

BioCyciLPNE297246:GCO9-2171-MONOMER.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR005105. GlnD_Uridyltrans_N.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[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]
ProtoNetiSearch...

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: Paris.

Entry informationi

Entry nameiGLND_LEGPA
AccessioniPrimary (citable) accession number: Q5X4J1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 23, 2004
Last modified: June 24, 2015
This is version 72 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

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.