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Q3JR26 (GLND_BURP1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:BURPS1710b_2585
OrganismBurkholderia pseudomallei (strain 1710b) [Complete proteome] [HAMAP]
Taxonomic identifier320372 [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_0000231679

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
Q3JR26 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: E71C618DBA6FE7F4

FASTA85896,750
        10         20         30         40         50         60 
MSASVAEPPP ALSRKAEFKA AKAELLARFK SANHVTPLMH ALSRATDDAL RSLWQECGLP 

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

       130        140        150        160        170        180 
VDQCIEEASH 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 ESFGYQPTSA 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 ALGMADARRF CREHGIEGDD AALVVWLVQH HLTMSQVAQK 

       550        560        570        580        590        600 
QDTSDPVVIK RFAELVGSER 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 EHDVQYRDIA NLVEQQLAAR LAESAPLPEP SKGRLSRLSR TFPITPRVDL 

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

       850 
DNRLQIQVET ELLRAIAV 

« Hide

References

[1]Woods D.E., Nierman W.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1710b.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000124 Genomic DNA. Translation: ABA50066.1.
RefSeqYP_333977.1. NC_007434.1.

3D structure databases

ProteinModelPortalQ3JR26.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING320372.BURPS1710b_2585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA50066; ABA50066; BURPS1710b_2585.
GeneID3688528.
KEGGbpm:BURPS1710b_2585.
PATRIC19237682. VBIBurPse115837_2711.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBPSE320372:GBYB-2585-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. 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_BURP1
AccessionPrimary (citable) accession number: Q3JR26
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: February 19, 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