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Q31G41 (GLND_THICR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. 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:Tcr_1287
OrganismThiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]
Taxonomic identifier317025 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesPiscirickettsiaceaeThiomicrospira

Protein attributes

Sequence length888 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 – 888888Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231696

Regions

Domain469 – 600132HD
Domain710 – 78778ACT 1
Domain817 – 88872ACT 2
Region1 – 348348Uridylyltransferase HAMAP-Rule MF_00277
Region349 – 709361Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q31G41 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 842AEC6110A9F414

FASTA888103,724
        10         20         30         40         50         60 
MATTTDKQVS PTSPSFVYNL DHEDRNTSLK SGRAVLTDFN EQQFVKFDKG CSIETLLKER 

        70         80         90        100        110        120 
TSFIDQLLKK IWEHFFSKDE CEQLTLVAVG GYGRGELQPY SDIDLLILGE NFIELQPKIV 

       130        140        150        160        170        180 
EFITYLWDIG FEVGHAVRNL EDCIEAGRED VTTATNLLEA RWLAGNYEQF LSLQNLFNLK 

       190        200        210        220        230        240 
SFWPSHEFFQ AKLEEQEKRH KRYNDTLYQL EPNIKESPGG LRDIQTILWV AKRHFGASSL 

       250        260        270        280        290        300 
QELMQHNFIS LQEYKEIQAA YLYLNRIRFA LHRLKKRHED RLLFDHQQQL AELLNHDDRP 

       310        320        330        340        350        360 
EHNDSIKAVE AFMKPYYQNA HIVARLNEIL LQHFKEEIYH FAEDKIEPIN PRFRIINNYL 

       370        380        390        400        410        420 
DVVKENLFAK NPTALLEIFI IIENYQHLIQ GIRSRTIRLI RNHLHLIDDQ FRSDPINKAL 

       430        440        450        460        470        480 
FIEIFRQPKG VNAAVKRMYA YGILGAYLPS FKKITGLMQF NIFHAYTVDE HTILVIRNLR 

       490        500        510        520        530        540 
RFFIKQHAYE FPTAHQIATQ LCKPEILLLA GLFHDIAKGR NGAHEKLGAV DAKAFSQKHN 

       550        560        570        580        590        600 
LNKNDTDLLS WLVLRHLDFS YVAQKKDLSD PEIIQQFAEK VGTQQRLDYL YLLTLADVRS 

       610        620        630        640        650        660 
TSDEVWNDWK NQLFLQLYHN TTQALDSSSS QPRDRVKQAI FNKEKASELL KKRGLIPMHF 

       670        680        690        700        710        720 
QGFWQAFEQT DFFNRQSAAE IARITRVLFE EDHEAINIHL QPTTSRGATE LIIYMHDRDY 

       730        740        750        760        770        780 
LFAQFTQIID KLDLNIVEAK IYSGEDDMTL VIIYLLNRES TSITDPMILT EIEETLKHQL 

       790        800        810        820        830        840 
FLKDDTMPPT QPEPRRIRVF EMPTHIQFQE INEELTELSI STKDIPGLLA KIGQAFKSCK 

       850        860        870        880 
IRVHDAKINT VGEKAEDTFM ISSTTNESIH TRHSQEELKQ ALLNNIEQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000109 Genomic DNA. Translation: ABB41882.1.
RefSeqYP_391556.1. NC_007520.2.

3D structure databases

ProteinModelPortalQ31G41.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING317025.Tcr_1287.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB41882; ABB41882; Tcr_1287.
GeneID3761676.
KEGGtcx:Tcr_1287.
PATRIC23974592. VBIThiCru83387_1340.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycTCRU317025:GHE8-1320-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]
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_THICR
AccessionPrimary (citable) accession number: Q31G41
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 6, 2005
Last modified: June 11, 2014
This is version 61 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