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Q667I7 (GLND_YERPS) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. 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:YPTB3005
OrganismYersinia pseudotuberculosis serotype I (strain IP32953) [Complete proteome] [HAMAP]
Taxonomic identifier273123 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length893 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 – 893893Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231699

Regions

Domain470 – 603134HD
Domain711 – 79383ACT 1
Domain819 – 89375ACT 2
Region1 – 351351Uridylyltransferase HAMAP-Rule MF_00277
Region352 – 710359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q667I7 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 8307CE87897AC85C

FASTA893103,172
        10         20         30         40         50         60 
MSDNHTEHSL SLTLTPTISE QPVLPSTYLD SDINCPILKQ RLDAFQRWQA EAFNSGTSAE 

        70         80         90        100        110        120 
VLIAARSDYI DHLLQRLWTF YGFDNVPETA LVAVGGYGRG ELHPLSDIDV LVLSKQRLND 

       130        140        150        160        170        180 
EHAQRVGQLI TLLWDLKLEV GHSVRTLEEC LLEGLADLTI ATNMIESRLI CGDVALFLQM 

       190        200        210        220        230        240 
QKHIFSDSFW PSPQFFHAKV VEQQERHKRY HGTSYNLEPD IKSSPGGLRD IHTLLWVARR 

       250        260        270        280        290        300 
HFGATSLSEM VDFGFLTNAE RNELNESQSF LWRIRFALHL VLTRYDNRLL FDRQLSVAQL 

       310        320        330        340        350        360 
LRYEGEGNEP VEHMMKDFYR MTRRVSELNN MLLQLFDEAI LALEANEKPR PLDEEFQLRG 

       370        380        390        400        410        420 
DLIDLRDENL FVRQPEAIMR MFYLMVRNQD IKGIYSTTVR RLRHARRHLK APLCHIPEAR 

       430        440        450        460        470        480 
KLFMAILRHP GAVSRALLPM HRHSVLWAYM PQWGSIVGQM QFDLFHAYTV DEHTIRVLLK 

       490        500        510        520        530        540 
IESFADEDTR PRHPLCVELY PRLPQPELLL LAALFHDIAK GRGGDHSILG AHDAVEFAEQ 

       550        560        570        580        590        600 
HGLNSRESQL VAWLVRCHLL MSVTAQRRDI QDPAVIQQFS AEVQSETRLR YLVSLTVADI 

       610        620        630        640        650        660 
CATNENLWNS WKQSLLRELY FATEKQLRRG MQNSPDLRER VRHHRLQALA LLRMDNIDEE 

       670        680        690        700        710        720 
ALHRIWSRCR ADYFLRHSPN QLAWHARHLL EHDSTKPLVL VSRQATRGGT EIFIWSPDRP 

       730        740        750        760        770        780 
SLFAAVVGEL DRRNLSVHDA QIFTNRDGMA MDTFIVLEPD GSPLAQDRHP IISHALQQAI 

       790        800        810        820        830        840 
NRSDYQHPPR VRRLSPKLRH FSVPTEANFL PTHNERRTYL ELIALDQPGL LARVGKIFAD 

       850        860        870        880        890 
LGLSLHSARI TTIGERVEDL FVLADKDRRA LSLETRRELA QRLADTLNPN DKL 

« Hide

References

[1]"Insights into the evolution of Yersinia pestis through whole-genome comparison with Yersinia pseudotuberculosis."
Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O., Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L., Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C., Simonet M., Chenal-Francisque V., Souza B. expand/collapse author list , Dacheux D., Elliott J.M., Derbise A., Hauser L.J., Garcia E.
Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IP32953.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX936398 Genomic DNA. Translation: CAH22243.1.
RefSeqYP_071511.1. NC_006155.1.

3D structure databases

ProteinModelPortalQ667I7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273123.YPTB3005.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAH22243; CAH22243; YPTB3005.
GeneID2955697.
KEGGyps:YPTB3005.
PATRIC18645193. VBIYerPse22266_3641.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycYPSE273123:GI1M-3106-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. 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_YERPS
AccessionPrimary (citable) accession number: Q667I7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 11, 2004
Last modified: June 11, 2014
This is version 70 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