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Q5LWE5 (GLND_RUEPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 72. 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:SPO0397
OrganismRuegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) [Complete proteome] [HAMAP]
Taxonomic identifier246200 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRuegeria

Protein attributes

Sequence length908 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 – 908908Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192769

Regions

Domain478 – 598121HD
Domain719 – 80183ACT 1
Domain829 – 90476ACT 2
Region1 – 360360Uridylyltransferase HAMAP-Rule MF_00277
Region361 – 718358Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q5LWE5 [UniParc].

Last modified February 1, 2005. Version 1.
Checksum: AA6C869FD08E01F5

FASTA908102,501
        10         20         30         40         50         60 
MFDTPAVFAR ITEAAAEAAD NAALRGAVVA ILRDVQNAGR AAIAEGFAED PFAARPLTRA 

        70         80         90        100        110        120 
YTYLTDGMVK TAMYVASEIL HPLATPTQGE RIAVLAVGGF GRGEMAPFSD VDLLFLTPYK 

       130        140        150        160        170        180 
ITAWAESVIE SMLYILWDLR LKVGHSSRTV KDCIRLGRDD FTIRTAMLEH RFLAGHAPLA 

       190        200        210        220        230        240 
RSLDQRLKSE LYKDTQREFI EAKLEERDAR HRKQGERYMV EPNVKEGKGG LRDLQSLYWI 

       250        260        270        280        290        300 
AKYIYEVKET AELVPLGLFT PSEYRTFVQA EEFLWAVRAH LHLVTGRATE QLTFDLQVEV 

       310        320        330        340        350        360 
AARMGYQDRA GRRGVEVFMQ KYFREATRVG ELTRIFLTKL EAAHMKGAPL LERIFRRRRR 

       370        380        390        400        410        420 
IKQGYKVVRG RLDVVDPEAF LADKLNLLRI FEEALRTGML IHPDAMRLVT ANLDLIDDGM 

       430        440        450        460        470        480 
RNDKEARRIF LDLLLKHGNP ERALRRMNEL GVLSAFVPEF EPIVAMMQFN MYHSYTVDEH 

       490        500        510        520        530        540 
TIQTIVNLAQ IEKGELVESL PLASSILKAG VNRKVLYVAL LLHDIGKGRP EDHSILGARI 

       550        560        570        580        590        600 
ARKVAPRLGL SKADCETVEW LVRYHLLMSD MAQKRDISDP RTVRDFAKAV QTTKRLDLLT 

       610        620        630        640        650        660 
VLTVCDIRGV GPNTWNNWKA TLLRALHAET KRALEMGMEA LNREGRGNEA KKALRTALSD 

       670        680        690        700        710        720 
WPAGEVKTEI ARHYPPYWQG FNVETHVTFA EMLRQLEHSG DPGGIEIRLD PDEDRDATRA 

       730        740        750        760        770        780 
CFAMADHPGI FSRMAGALAL VGANVVDARS YTTKDGYVTD AFWIQDAEGH PYEAARLPRL 

       790        800        810        820        830        840 
SQMILKTLKG EVVARDALKS RDKIKKREKA FNVPTHITFD NEGSDIYTII EVDTRDRPGL 

       850        860        870        880        890        900 
LYDLARALAA ANVYIANAVI ATYGEQVVDS FYVKDMFGLK YHSEAKQRTL ETKLRKAITE 


GAERAAAS 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000031 Genomic DNA. Translation: AAV93715.1.
RefSeqYP_165660.1. NC_003911.12.

3D structure databases

ProteinModelPortalQ5LWE5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246200.SPO0397.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV93715; AAV93715; SPO0397.
GeneID3195406.
KEGGsil:SPO0397.
PATRIC23374055. VBIRuePom114501_0404.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 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_RUEPO
AccessionPrimary (citable) accession number: Q5LWE5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: February 1, 2005
Last modified: June 11, 2014
This is version 72 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