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Q2SX00 (GLND_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. 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:BTH_I2025
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

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_1000022336

Regions

Domain444 – 550107HD
Domain682 – 76180ACT 1
Domain790 – 85869ACT 2
Region1 – 324324Uridylyltransferase HAMAP-Rule MF_00277
Region325 – 681357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q2SX00 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 80780D220D54F576

FASTA85896,880
        10         20         30         40         50         60 
MSASVAAPPP ALSRKAEFKA AKAELLARFQ TATNVTPLMH ALSRATDDAL RRLWHECGLP 

        70         80         90        100        110        120 
ATLALVAVGG FGRGELSPHS DVDILVLLPD AHARELDERI ERFIGMAWDL GLEIGSSVRT 

       130        140        150        160        170        180 
VDQCIEEASQ DVTVQTSLLE ARRIVGSTAL FERFMLRYRE ALDARAFFQA KVLEMRQRHA 

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

       250        260        270        280        290        300 
GFLKTLRARL HVIAGRRQDI LVFDLQTQAA ESFGYRPTPA KRASEQLMRR YYWAAKAVTQ 

       310        320        330        340        350        360 
LATILIQNIE AQLFPATSGV TRVLSPGRFV EKQGMLEIAA DDVFERHPDA ILEAFLLYEA 

       370        380        390        400        410        420 
TRGVKGLSAR TLRALYNSRD VMNNAWRRDP RNRHTFMQIL QQPEGITHAF RLMNQTSVLG 

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

       490        500        510        520        530        540 
VLYVAALFHD IAKGRGGDHS ALGMTDARRF CREHGIEGGD AALVVWLVQH HLTMSQVAQK 

       550        560        570        580        590        600 
QDTSDPEVIK RFADLVGNER RLTALYLLTV ADIRGTSPKV WNTWKGKLLE DLYRATLAVL 

       610        620        630        640        650        660 
GGAQPDAHSE LKTRQEEALA LLRLETVPPD AHRALWDQLD VGYFLRHDAA DIAWQTRVLY 

       670        680        690        700        710        720 
RHVAADTAIV RARPSPVGDA LQVLVYVKDR SDLFAGICAY FDRNGLSVLD ARVNTTRHGY 

       730        740        750        760        770        780 
ALDNFIVTQT ERDVQYRDIA NLVEQQLAAR LAESAPLPEP SKGRLSRLSR TFPITPRVDL 

       790        800        810        820        830        840 
RADERGQYYI LSVSANDRPG LLYSIARVLA EHRVGVHAAR INTLGERVED VFMLDGTGLS 

       850 
DNRLQIQVET ELLRAIAV 

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References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC39424.1.
RefSeqYP_442549.1. NC_007651.1.

3D structure databases

ProteinModelPortalQ2SX00.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING271848.BTH_I2025.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC39424; ABC39424; BTH_I2025.
GeneID3848603.
KEGGbte:BTH_I2025.
PATRIC19307090. VBIBurTha36512_4834.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycBTHA271848:GJMY-2026-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_BURTA
AccessionPrimary (citable) accession number: Q2SX00
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: June 11, 2014
This is version 66 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