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B1YS76 (GLND_BURA4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:BamMC406_1923
OrganismBurkholderia ambifaria (strain MC40-6) [Complete proteome] [HAMAP]
Taxonomic identifier398577 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia 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 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 – 858858Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000114751

Regions

Domain444 – 548105HD
Domain682 – 76180ACT 1
Domain790 – 85869ACT 2
Region1 – 324324Uridylyltransferase HAMAP-Rule MF_00277
Region325 – 681357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
B1YS76 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 06055B9E8D5CCD32

FASTA85897,013
        10         20         30         40         50         60 
MSAHAAPSSE ALSRRAEFKA AKADMLERFR SAANVASLMH ALSKLTDDAL KRVWDDCGLP 

        70         80         90        100        110        120 
ATLALIAVGG YGRGELAPYS DVDILVLLPD AHDPALDARI ERFIGMAWDL GLEIGSSVRT 

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

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

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

       310        320        330        340        350        360 
LATILIQNIE AQLFPATSGI TRVLSPDRFV EKQGMLEIVD DGVFERHPDA ILEAFLLYEV 

       370        380        390        400        410        420 
TRGVKGLSAR TLRALYNSRE IMNNTWRRDP QNRRTFMQIL QQPEGITHAF RLMNQTSVLG 

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

       490        500        510        520        530        540 
VLYVAALFHD IAKGRGGDHS TLGMADARRF CREHGITGDD 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 LAETAPLPEP SKGRLSRLSR TFPITPRVDL 

       790        800        810        820        830        840 
RADERGQYYI LSVSANDRPG LLYSIARVLA EHQVGVHAAR INTLGERVED IFLLDGAGLS 

       850 
DNRLQIQLET ELLRAIAV 

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References

[1]"Complete sequence of chromosome 1 of Burkholderia ambifaria MC40-6."
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A. expand/collapse author list , Ramette A., Konstantinidis K., Tiedje J., Richardson P.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC40-6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001025 Genomic DNA. Translation: ACB64405.1.
RefSeqYP_001808621.1. NC_010551.1.

3D structure databases

ProteinModelPortalB1YS76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398577.BamMC406_1923.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB64405; ACB64405; BamMC406_1923.
GeneID6177328.
KEGGbac:BamMC406_1923.
PATRIC19033308. VBIBurAmb82852_1973.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBAMB398577:GH38-1972-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_BURA4
AccessionPrimary (citable) accession number: B1YS76
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 46 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