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A1JP85 (GLND_YERE8) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 56. 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:YE3286
OrganismYersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) [Complete proteome] [HAMAP]
Taxonomic identifier393305 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length892 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 – 892892Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000022356

Regions

Domain470 – 603134HD
Domain711 – 79282ACT 1
Domain818 – 89275ACT 2
Region1 – 351351Uridylyltransferase HAMAP-Rule MF_00277
Region352 – 710359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A1JP85 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: F9A01583B3D41D50

FASTA892103,044
        10         20         30         40         50         60 
MSDNHTEHSV LPAVTKVIPE QPASPATYLD SELNCPELKQ RLETFQSWLA DAFNGGISAE 

        70         80         90        100        110        120 
TLIAARSDYI DRLLGRLWTF YGFDDVPETA LVAVGGYGRG ELHPLSDIDV LILSKQRLND 

       130        140        150        160        170        180 
EHAQRVGQLI TLLWDLKLEV GHSVRTLEEC LLEGLADLTV ATNMVESRLI CGDVALFLQM 

       190        200        210        220        230        240 
QKHIFSDNFW PSPKFFHAKV VEQQERHKRY HGTSYNLEPD IKSSPGGLRD IHTLQWVARR 

       250        260        270        280        290        300 
HFGATSLSEM VDFGFLTKAE RNELIESQSF LWRIRFALHL VLTRYDNRLL FDRQLSVAQL 

       310        320        330        340        350        360 
LQYQGEGNEP VERMMKDFYR MTRRVSELNN MLLQLFDEAI LALDTNEKPR PLDDEFQLRG 

       370        380        390        400        410        420 
DLIDLRDENL FVDKPEAIMR MFYLMVRNQD IKGIYSTTVR RLRHARRHLK QPLCNIPEAR 

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

       490        500        510        520        530        540 
LESFADESTR PRHPLCVELY PRLPQPELLL LAALFHDIAK GRGGDHSILG AHDVLEFAEQ 

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

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

       670        680        690        700        710        720 
ALHHIWSRCR ADYFLRHSPN QLAWHARHLL EHDSTKPLVL VSRQATRGGT EIFIWCPDRP 

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

       790        800        810        820        830        840 
TRQNYQHPRV RRLSPKLRHF SVPTETNFLP THNERRTYLE LIALDQPGLL ARVGDIFADL 

       850        860        870        880        890 
GLSLHSARIT TIGERVEDLF VLADKDRRAL SIETRRELAQ RLTDTLNPND KL 

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References

[1]"The complete genome sequence and comparative genome analysis of the high pathogenicity Yersinia enterocolitica strain 8081."
Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L., Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T., Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S., Sanders M., Whitehead S. expand/collapse author list , Quail M.A., Dougan G., Parkhill J., Prentice M.B.
PLoS Genet. 2:2039-2051(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 13174 / 8081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM286415 Genomic DNA. Translation: CAL13316.1.
RefSeqYP_001007460.1. NC_008800.1.

3D structure databases

ProteinModelPortalA1JP85.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING393305.YE3286.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAL13316; CAL13316; YE3286.
GeneID4713381.
KEGGyen:YE3286.
PATRIC18566317. VBIYerEnt11519_3496.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
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. 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_YERE8
AccessionPrimary (citable) accession number: A1JP85
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 56 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