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B1JUF2 (GLND_BURCC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:Bcenmc03_2041
OrganismBurkholderia cenocepacia (strain MC0-3) [Complete proteome] [HAMAP]
Taxonomic identifier406425 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex ›

Protein attributes

Sequence length858 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 – 858858Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000114752

Regions

Domain444 – 548105HD
Domain682 – 76382ACT 1
Domain790 – 85869ACT 2
Region1 – 324324Uridylyltransferase HAMAP-Rule MF_00277
Region325 – 681357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
B1JUF2 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: E85B86E5A00DF810

FASTA85896,854
        10         20         30         40         50         60 
MSAHAAPSPE ALSRRAEFKA AKTEMLERFR HAANVASLMH ALSKLTDDAL KRVWDECGLP 

        70         80         90        100        110        120 
ATLALVAVGG YGRGELAPYS DVDIVVLLPD AHDAALDARI ERFIGMAWDL GLEIGSSVRT 

       130        140        150        160        170        180 
VAQCIEEASQ DVTVQTSLLE ARRIVGSTAL FERFTVRYHE ALDARAFFTA KVLEMRQRHA 

       190        200        210        220        230        240 
KFQDTPYSLE PNVKESPGGL RDLQTILWIA RAAGFGSSWR ELDTRGLITD REARELRRNE 

       250        260        270        280        290        300 
GFLKTLRARL HVIAGRRQDM LVFDLQTQAA ESFGYQPTQA KRASEQLMRR YYWAAKAVTQ 

       310        320        330        340        350        360 
LATILIQNIE AQLFPATSGI TRVLSADRFV EKQGMLEIVD DGVFERHPDA ILEAFLLYET 

       370        380        390        400        410        420 
TRGVKGLSAR TLRALYNSRE IMNNAWRRDP QNRATFMRIL QQPEGITHAF RLMNQTSVLG 

       430        440        450        460        470        480 
RYLLNFRRIV GQMQHDLYHV YTVDQHILMV LRNIRRFAVA EHAHEYPFCS QLIGNFERPW 

       490        500        510        520        530        540 
ALYVAALFHD IAKGRGGDHS TLGMADARRF CREHGIAGDD AALIVWLVQH HLTMSQVAQK 

       550        560        570        580        590        600 
QDTSDPEVIK RFAEVVGNER YLTALYLLTV ADIRGTSPKV WNTWKGKLLE DLYRITLAVL 

       610        620        630        640        650        660 
GGANPDAHSE LKSRQEQALA LLRLETVPDD AHRALWDQLD VGFFLRHDAA DIAWQTRVLY 

       670        680        690        700        710        720 
RHVNAETAIV RARPSPIGDA LQVLVYVKDR PDLFAGICAY FDRNGLSVLD ARVSTTRHGY 

       730        740        750        760        770        780 
ALDNFIVTQT ERDVRYRDIA NLVEQQLATR LAETASLPEP SKGRLSRLSR TFPITPRVDL 

       790        800        810        820        830        840 
RADERGQYYI LSVSANDRPG LLYSIARVLA EHRIGVHAAR INTLGERVED IFLLAGAGLS 

       850 
DNRLQIQLET ELLRAIAV

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References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3."
Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Tiedje J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC0-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000958 Genomic DNA. Translation: ACA91202.1.
RefSeqYP_001765324.1. NC_010508.1.

3D structure databases

ProteinModelPortalB1JUF2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING406425.Bcenmc03_2041.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA91202; ACA91202; Bcenmc03_2041.
GeneID6123705.
KEGGbcm:Bcenmc03_2041.
PATRIC19091213. VBIBurCen61509_2111.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBCEN406425:GHD9-2092-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_BURCC
AccessionPrimary (citable) accession number: B1JUF2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 29, 2008
Last modified: February 19, 2014
This is version 43 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

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