Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A5ICM0 (GLND_LEGPC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. [Protein-PII] uridylyltransferase
    Short name=PII uridylyltransferase
    Short name=UTase
    EC=2.7.7.59
  2. [Protein-PII]-UMP uridylyl-removing enzyme
    Short name=UR
    EC=3.1.4.-
Gene names
Name:glnD
Ordered Locus Names:LPC_1154
OrganismLegionella pneumophila (strain Corby) [Complete proteome] [HAMAP]
Taxonomic identifier400673 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length861 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00277

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP-Rule MF_00277

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. HAMAP-Rule MF_00277

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00277

Enzyme regulation

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity. HAMAP-Rule MF_00277

Domain

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. HAMAP-Rule MF_00277

Sequence similarities

Belongs to the GlnD family.

Contains 2 ACT domains.

Contains 1 HD domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 861861Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000022345

Regions

Domain441 – 570130HD
Domain679 – 76082ACT 1
Domain788 – 86174ACT 2
Region1 – 321321Uridylyltransferase HAMAP-Rule MF_00277
Region322 – 678357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A5ICM0 [UniParc].

Last modified June 26, 2007. Version 1.
Checksum: 5D4C195868AFC94F

FASTA861100,711
        10         20         30         40         50         60 
MKNDNRIIKN TIKQFKEKLC KDFSQKANIT SITRKLAVFI DTILIQLFIK NKLHFGDNFC 

        70         80         90        100        110        120 
LLALGSYGRR ELQLHSDIDL LILHTEKVSN IQLQRAQKFI QDCWDVGLEV SHQITTVSSC 

       130        140        150        160        170        180 
ANLASQDLSV ISTIMDMFLL CGHGALMEEL IYQTHTLHMW PSHQYFFAKL QEQQNRYAKY 

       190        200        210        220        230        240 
GETAYNLEPN IKNGPGGLRD LQILLSISKR HFKIKKLAEG IGYGFITDKE YEELKYCQNF 

       250        260        270        280        290        300 
LWRVRFALHM LAGKPEERLS FDYQVKLAQF FGYQDQSHIL AIEQFMKDYF KVIKRNRELN 

       310        320        330        340        350        360 
EMLLQWFNET IVYHQKQKII RLDDEFQLSN RFIEVRNNRV FKQNPQSILK LFYWLVKRPD 

       370        380        390        400        410        420 
IEGVRASTIR LIRESLFLMG KRFRESKETA NIFINIFRTG NDPYDALQRM NRYGVLAHYL 

       430        440        450        460        470        480 
DCFATATGQM QYDLFHAYTV DQHTLFVIRN ISRFKKNEYA KQFPLCAKII TALEKPEILY 

       490        500        510        520        530        540 
LGALFHDIAK GRGGDHSELG AIEAQQFTQR HYMEAEDSKL IVWLVRYHLL MSQTAQRKDI 

       550        560        570        580        590        600 
YDPKTIEQFC QLLPHARYLD YLYLLTVADI CGTNPTLWNA WKDSLLKELY HAAKTRLHKQ 

       610        620        630        640        650        660 
QELLDEAALI SIRKQYAMDI LISDGISSRV IQDLWSQFKG KYFLHESPEV IARHTKAILN 

       670        680        690        700        710        720 
SKQFPVVIIM PHHSQGGTEV FIYMPHKDER FTITTSVLSN HHVTIQEAAI ITCDNQFDLD 

       730        740        750        760        770        780 
TYIILDENNQ AFLNEQRARD IQKNLCDHLA NTGRLPAVSR RRLSRALTHF NVKTQINFID 

       790        800        810        820        830        840 
DNTNHQTQLF LVTNDRPGLL ATISRVFLTL NIHLHNAKIA TAGERVEDMF YISNQTGYSL 

       850        860 
NHEEKTILKE KLILEISKSK Y 

« Hide

References

[1]"Identification and characterization of a new conjugation/ type IVA secretion system (trb/tra) of L. pneumophila Corby localized on a mobile genomic island."
Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E., Steinert M., Buchrieser C., Hacker J., Heuner K.
Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Corby.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000675 Genomic DNA. Translation: ABQ55120.1.
RefSeqYP_001250466.1. NC_009494.2.

3D structure databases

ProteinModelPortalA5ICM0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING400673.LPC_1154.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ55120; ABQ55120; LPC_1154.
GeneID5180977.
KEGGlpc:LPC_1154.
PATRIC22308727. VBILegPne45588_1196.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBCLSK832981.

Enzyme and pathway databases

BioCycLPNE400673:GCIT-1827-MONOMER.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR005105. GlnD_Uridyltrans_N.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF03445. DUF294. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
[Graphical view]
PIRSFPIRSF006288. PII_uridyltransf. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR01693. UTase_glnD. 1 hit.
PROSITEPS51671. ACT. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLND_LEGPC
AccessionPrimary (citable) accession number: A5ICM0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 26, 2007
Last modified: February 19, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families