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A4JF78 (GLND_BURVG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:Bcep1808_1928
OrganismBurkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia (strain R1808)) [Complete proteome] [HAMAP]
Taxonomic identifier269482 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length859 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 fixation 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 – 859859Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000022337

Regions

Domain445 – 546102HD
Domain683 – 76280ACT 1
Domain791 – 85969ACT 2
Region1 – 325325Uridylyltransferase HAMAP-Rule MF_00277
Region326 – 682357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A4JF78 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: AD7EF37E58B2FD88

FASTA85997,064
        10         20         30         40         50         60 
MSAHAAPSPE ALSRRAEFKA AKADLLERFR SATNVTSLMH ALSKLTDSAL KRVWDDCGLP 

        70         80         90        100        110        120 
ATLALVAVGG YGRGELAPHS DVDILVLLPD AHDPALDARI ERFIGMAWDL GLEIGSSVRT 

       130        140        150        160        170        180 
VAQCIEEASQ DVTVQTSLLE ARRIFGSTAL FERFTVRYHE EALDARAFFT AKVLEMRQRH 

       190        200        210        220        230        240 
AKFQDTPYSL EPNVKESPGG LRDLQTILWI ARAAGFGSSW RELDTRGLIT EREARELRRN 

       250        260        270        280        290        300 
EGFLKALRAR LHVIAGRRQD VLVFDLQTQA AESFGYRPTQ AKRASEQLMR RYYWAAKAVT 

       310        320        330        340        350        360 
QLATILIQNI EAQLFPATSG ITRVLSHDRF VEKQGMLEIV DDGVFERHPD AILEAFLLYE 

       370        380        390        400        410        420 
TTRGVKGLSA RTLRALYNSR EIMNDTWRRD AQNRHTFMQI LQQPEGITHA FRLMNQTSVL 

       430        440        450        460        470        480 
GRYLLNFRRI VGQMQHDLYH VYTVDQHILM VLRNIRRFAV AEHAHEYPFC SQLIGNFERP 

       490        500        510        520        530        540 
WVLYVAALFH DIAKGRGGDH STLGMADARR FCREHGIGGD DAALIVWLVQ HHLTMSQVAQ 

       550        560        570        580        590        600 
KQDTSDPEVI KRFAAIVGNE RYLTALYLLT VADIRGTSPK VWNTWKGKLL EDLYRITLAV 

       610        620        630        640        650        660 
LGGAKPDAHS ELKSRQEQAL ALLRLETVPD DAHRALWDQL DVGFFLRHDA ADIAWQTRVL 

       670        680        690        700        710        720 
YRHVNAETAI VRARPSPIGD ALQVLVYVKD RPDLFAGICA YFDRNGLSVL DARVSTTRHG 

       730        740        750        760        770        780 
YALDNFIVTQ TERDVRYRDI ANLVEQQLAT RLAETAPLPE PSKGRLSRLS RTFPITPRVD 

       790        800        810        820        830        840 
LRADERGQYY ILSVSANDRP GLLYSIARVL AEHRVGVHAA RINTLGERVE DIFLLDGAGL 

       850 
SDNRLQIQLE TELLRAIAV 

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References

[1]"Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Tiedje J., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: G4 / LMG 22486.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000614 Genomic DNA. Translation: ABO54931.1.
RefSeqYP_001119766.1. NC_009256.1.

3D structure databases

ProteinModelPortalA4JF78.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269482.Bcep1808_1928.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO54931; ABO54931; Bcep1808_1928.
GeneID4953651.
KEGGbvi:Bcep1808_1928.
PATRIC19322457. VBIBurVie89221_6191.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK03059.

Enzyme and pathway databases

BioCycBVIE269482:GJNA-1978-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_BURVG
AccessionPrimary (citable) accession number: A4JF78
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 1, 2007
Last modified: February 19, 2014
This is version 54 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