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Q7VYD2 (GLND_BORPE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. 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:BP1417
OrganismBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) [Reference proteome] [HAMAP]
Taxonomic identifier257313 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length865 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 – 865865Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192720

Regions

Domain438 – 544107HD
Domain676 – 76287ACT 1
Domain789 – 86577ACT 2
Region1 – 318318Uridylyltransferase HAMAP-Rule MF_00277
Region319 – 675357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q7VYD2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: D8E17E5527129A45

FASTA86598,524
        10         20         30         40         50         60 
MPHVDLNPLK QRMQAARAAA VAQFRQHPRP DMLLTELRRI VDQALRELVK LCPLPAGATL 

        70         80         90        100        110        120 
AAVGSYGRGE LYPHSDVDLL ILLPQPPSAA DARAVEALVA ALWDLGLEPG HSVRTLEDCE 

       130        140        150        160        170        180 
REARGDITVE TALLESRWLA GSRTLMKRLD SAMQARLDAA VFFQAKRVEM QQRHAHYQDT 

       190        200        210        220        230        240 
PYALEPNCKE SPGGLRDLQV ILWMARAAGF GHSWREVAQA GLLTSSEARD LRRAEQAFKR 

       250        260        270        280        290        300 
LRIELHLLTG RREDRVLFDL QPGLAAVYGI ASTATRRASE LLMQRYYWAA RLVTQLNVIL 

       310        320        330        340        350        360 
VQNIEERLFP RPDSDARLID DDFRNLRERL DIVREDGFER NPTLLLRAFL VMQQHPELIG 

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

       430        440        450        460        470        480 
RRIVGQMQHD LFHVYTVDQH TLAVVRNLRR FTMPEHAQEY PLASQLIAGL DRHWLLYVAA 

       490        500        510        520        530        540 
LFHDIAKGRG GDHSELGARE VRRFAQDHGL DPTDAELVEF LVRHHLLMSA VAQKRDLSDP 

       550        560        570        580        590        600 
QVVRDFAAQV GDERRLAALY LLTVADIRGT SPRVWNAWKG KLLEDLFRLT LAALGGAHAD 

       610        620        630        640        650        660 
AHTVLTERKD EAARLTRLAG LRDDAREAFW NQLDIAYFLR HDASEIAWHT RHLYYQVAPD 

       670        680        690        700        710        720 
EPVVRVRPTE HGEGLQVMVY TRDAPDLFVT TCGYFDAKSL SVQDARVHTT RHGWALDSFI 

       730        740        750        760        770        780 
VLAPEGFADL RAQATLVEHE LAERLRDPHA ARHAHAPRRL PHSHARRSRV FPVMPQAELS 

       790        800        810        820        830        840 
PDERSQSWRL SVTATDRPGL LYALARVFAE HGVDLIMAKI MTLGERVEDV FIVSGSALER 

       850        860 
PRSQMQFERA ILDALAGDEP RQQAA 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX640415 Genomic DNA. Translation: CAE41707.1.
RefSeqNP_880159.1. NC_002929.2.

3D structure databases

ProteinModelPortalQ7VYD2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING257313.BP1417.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE41707; CAE41707; BP1417.
GeneID2667683.
KEGGbpe:BP1417.
PATRIC21156046. VBIBorPer7866_1519.

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycBPER257313:BP1417-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_BORPE
AccessionPrimary (citable) accession number: Q7VYD2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 69 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