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Q470D5 (GLND_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 62. 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:Reut_A1883
OrganismCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Ralstonia eutropha (strain JMP 134)) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length869 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 – 869869Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231689

Regions

Domain451 – 54898HD
Domain689 – 77385ACT 1
Domain800 – 86970ACT 2
Region1 – 331331Uridylyltransferase HAMAP-Rule MF_00277
Region332 – 688357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q470D5 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 8028D86E94BE91AE

FASTA86998,722
        10         20         30         40         50         60 
MPTNLPALPM DTTPELLLAA RVRDQLKADK QALFADFDLS SHVGTLVTRL RRAVDAALAE 

        70         80         90        100        110        120 
AWRGLDMPAD AALVAVGGYG RGELFPYSDV DVLLLLRAEP DADTVSRLER FIGMCWDLGL 

       130        140        150        160        170        180 
EIGSSVRTVE DCIREARADI TIQTSLLEAR LLTGNRKLFE ALRTQHQADL DPAAFFQAKL 

       190        200        210        220        230        240 
LEMRQRHAKY QDTPYALEPN CKESPGGLRD LQVILWMTKA AGLGDSWKEL FERGLLTQRE 

       250        260        270        280        290        300 
AQELSRNERL LKTIRARLHL VAGRRQDVLV FDLQTALAES FGYRQNANKR ASEQLMRRYF 

       310        320        330        340        350        360 
WAAKAVTQLN SVLLLNIEAL LFPSESQVTR VINERFVERQ GMLEITSDSL YEDDPHAILE 

       370        380        390        400        410        420 
TFLLYERTPG IKGLSPRTLR GLYNARTVMD ARWRSDPENR RLFLAILQEP QGITHALRLM 

       430        440        450        460        470        480 
NQTSVLGRYL INFRRIVGQM QHDLFHVYTV DQHILMVVRN MRRFAIVEHT HEFPFCSQLM 

       490        500        510        520        530        540 
ASFDKPWVLS VAALFHDIAK GRGGDHSKLG TVDARRFCKQ HGIGREDADL ICWLVEHHLT 

       550        560        570        580        590        600 
MSHVAQKQDL TDPDVVHAFA RVVGDERHLT ALYLLTVADV RGTSPKVWNA WKGKLLEDLY 

       610        620        630        640        650        660 
RITLRVLGGA RVDPHSIWAQ RQEETISQLR LKAFDPELGK PLWAQLDVAF FLRHDSRDIA 

       670        680        690        700        710        720 
WLTRHLFNKV DSPVPVVKAR ISPAGEGLQV AVYVKDQPDL FARICGYFER KAFSIQDAKI 

       730        740        750        760        770        780 
HTTRHGYALD TFQVTDPGLA DDGGNYRDIL ALVEHELGDR LQQQAALPEP SQGRLSRQSR 

       790        800        810        820        830        840 
SFPIKPRVDL RPDERGQYYL LSLSANDRTG LLYAITRVLA KHRVSVHTAR INTLGERVED 

       850        860 
VFLVDGSRLA ADNRLQIQLE QDLLAALEI 

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References

[1]"Complete sequence of chromosome 1 of Ralstonia eutropha JMP134."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JMP134 / LMG 1197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000090 Genomic DNA. Translation: AAZ61248.1.
RefSeqYP_296092.1. NC_007347.1.

3D structure databases

ProteinModelPortalQ470D5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING264198.Reut_A1883.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ61248; AAZ61248; Reut_A1883.
GeneID3609562.
KEGGreu:Reut_A1883.
PATRIC20229317. VBIRalEut24049_2517.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-1903-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_CUPPJ
AccessionPrimary (citable) accession number: Q470D5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2005
Last modified: June 11, 2014
This is version 62 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