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Q2NRK5 (GLND_SODGM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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:SG1945
OrganismSodalis glossinidius (strain morsitans) [Complete proteome] [HAMAP]
Taxonomic identifier343509 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSodalis

Protein attributes

Sequence length896 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 – 896896Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000204801

Regions

Domain474 – 607134HD
Domain715 – 79682ACT 1
Domain822 – 89675ACT 2
Region1 – 355355Uridylyltransferase HAMAP-Rule MF_00277
Region356 – 714359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q2NRK5 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 2BAC301F1C44FF4D

FASTA896103,328
        10         20         30         40         50         60 
MQGDPMPDQI LQFTHPPVPR QPPVKPSSPL TWPDDALNRP FLKERLDEFQ RWLADAFDAG 

        70         80         90        100        110        120 
ETAEILVDAR TLYIDQLLRQ LWHYHGLAHA PHTALVAVGG YGRGELHPLS DIDVLVLSQA 

       130        140        150        160        170        180 
PLTPPQQQHI SELLTLLWDL KLEVGHSVRS IAECLEEGRA DLTVATNLIE SRLICGDLAL 

       190        200        210        220        230        240 
FLTLQKQVFS DDFWPSRAFF PAKLAEQQER HSRYHGTSYN LEPDIKSSPG GLRDIHTLLW 

       250        260        270        280        290        300 
VAHRHFGATS MDEMVGFGFI TRAERDELNE CQSFLWRTRF ALHLVLNRYD NRLLFDRQQN 

       310        320        330        340        350        360 
VAQLLRYQGE GNLPVERMMK DFFRVTRRVS ELNQMLLQLF DEAILALAPD EKPQPLDDEF 

       370        380        390        400        410        420 
QLRGNLIDLR DETLFSRQPE AILLLFWQMV RNRHIEGIYS ATLRQLRYAR RHLKAPLCTS 

       430        440        450        460        470        480 
PEARTLFMRI LHQPGAVKHA LLPMHRHSVL WAYMPQWSNI VGQMQFDLFH AYTVDEHTIR 

       490        500        510        520        530        540 
VLLKLESFAD ESQRPYHPLC VELFPRLSQR HLLLVAALFH DIAKGRGGDH SQLGARDVLE 

       550        560        570        580        590        600 
FAALHDLPAE DAQLVAWLVE SHLVMSVTAQ RRDIQEPDVL VQFAGEMQSE SRLHYLLCLT 

       610        620        630        640        650        660 
VADICATNET LWNSWKQSLL RELFFATEKQ LRRGIHVSPD VRERVRHNRR QSLVLLRMEG 

       670        680        690        700        710        720 
IDEQRLQEIW SRCRADYFLR HTPNQLAWHA RHMVLHDHDE PLVLISPQAT RGGTEIFIHN 

       730        740        750        760        770        780 
QDRPYLFAAV TGELDRRNLS VHDAQIFTNR DGMAMDTFVV LEPDGSPLSP DRHPVIRQAL 

       790        800        810        820        830        840 
LQILLPGDYR HPRVRRPSSK LRHFNVDTSV VFLPSPTERR SYLELTALDQ PGLLARVSEV 

       850        860        870        880        890 
FVDLGISLHG ARISTIGERV EDLFILADGD RRALSRAMQA EVRRRLTEAL NPNDKV 

« Hide

References

[1]"Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."
Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.
Genome Res. 16:149-156(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: morsitans.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008232 Genomic DNA. Translation: BAE75220.1.
RefSeqYP_455625.1. NC_007712.1.

3D structure databases

ProteinModelPortalQ2NRK5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING343509.SG1945.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE75220; BAE75220; SG1945.
GeneID3867857.
KEGGsgl:SG1945.
PATRIC23654843. VBISodGlo61428_4706.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05007.

Enzyme and pathway databases

BioCycSGLO343509:GJJC-2011-MONOMER.

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]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 2 hits.
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_SODGM
AccessionPrimary (citable) accession number: Q2NRK5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 7, 2006
Last modified: February 19, 2014
This is version 67 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