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Q2L165 (GLND_BORA1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:BAV1732
OrganismBordetella avium (strain 197N) [Complete proteome] [HAMAP]
Taxonomic identifier360910 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

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_1000022326

Regions

Domain438 – 550113HD
Domain675 – 75682ACT 1
Domain789 – 85870ACT 2
Region1 – 318318Uridylyltransferase HAMAP-Rule MF_00277
Region319 – 674356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q2L165 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: DE261EA92F0D5AB7

FASTA85897,978
        10         20         30         40         50         60 
MNPTDLHPIK ERMQAARAAA IADFRQHLRP DPLLSELRRI VDQALRDLLK LCPLPAGATL 

        70         80         90        100        110        120 
AAVGGYGRGE LYPHSDVDLL ILLPRAPDGP DESAIETLVA SLWDLGLEPG HSVRTLAECE 

       130        140        150        160        170        180 
TEASADITVE TALLESRWLA GSRSLMKQFE TAMTARLDAR AFFRAKRVEM QQRHARYQDT 

       190        200        210        220        230        240 
PYALEPNSKE SPGGLRDLQV ILWMARAAGF GRNWRAVAQA GLLTAPEARD LRRAEQAFKR 

       250        260        270        280        290        300 
LRIELHLLTR RREDRLLFDL QPTLAEVYGI ATTTTRRASE LLMQRYYWAA RLVTQLNVIL 

       310        320        330        340        350        360 
IQNIEERLFP RPESDARAID EEFRSLHGRL DIIREDCFER NPTLLLRAFL VMQQHPGLSG 

       370        380        390        400        410        420 
MSARTLRAIW HSRHRIDAQF RRNPVNRKLF LQILQQPRGI VHELRRMTML NILPRYLPVF 

       430        440        450        460        470        480 
RRIVGQMQHD LFHVYTVDQH TLAVIRNLRR FTMPEHASEY PLASQVMAGL DRHWLLYVAA 

       490        500        510        520        530        540 
LFHDIAKGRG GDHSELGARD ARRFAQEHGL APEDAELVEF LVRQHLLMSA VAQKRDLSDP 

       550        560        570        580        590        600 
EVINEFARQV KDERHLNALY LLTVADIRGT SPKVWNAWKG KLLEDLYRLT LAALGGAQDT 

       610        620        630        640        650        660 
RTVLAERKEE AARLLRLAGL RDDARDAFWQ QLDVAYFLRH DASEIAWHTR HLYYQVQPDK 

       670        680        690        700        710        720 
PVVKVRPTEE GSGLQIMVYT RDTPDLFMNT CAYFDGKAFS IQDARIHTTR QGWALDSFIV 

       730        740        750        760        770        780 
LPAEPLADLR AQAALVEHEL AERLRQAQGG ARLADVRVFH RNRQSRVSRV FPVMPQAELH 

       790        800        810        820        830        840 
PDERSQSWRL SVTATDRPGL LHALARVMAE NGVNLIMAKI MTLGDRVEDV FIISGAVLER 

       850 
PRTQMQFEHA VLDALAGE 

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References

[1]"Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 197N.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM167904 Genomic DNA. Translation: CAJ49340.1.
RefSeqYP_786250.1. NC_010645.1.

3D structure databases

ProteinModelPortalQ2L165.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360910.BAV1732.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6266904.
KEGGbav:BAV1732.
PATRIC21129646. VBIBorAvi43433_1744.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBAVI360910:GCKI-1759-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_BORA1
AccessionPrimary (citable) accession number: Q2L165
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: February 19, 2014
This is version 63 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