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Q3SKP1 (GLND_THIDA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:Tbd_0783
OrganismThiobacillus denitrificans (strain ATCC 25259) [Complete proteome] [HAMAP]
Taxonomic identifier292415 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeThiobacillus

Protein attributes

Sequence length850 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 – 850850Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231695

Regions

Domain437 – 546110HD
Domain674 – 75582ACT 1
Domain783 – 85068ACT 2
Region1 – 317317Uridylyltransferase HAMAP-Rule MF_00277
Region318 – 673356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q3SKP1 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: AA673373E9F73EE8

FASTA85095,305
        10         20         30         40         50         60 
MSARPFADLR ERLKSGRASL AAAYREKPRA AHYLARHAAL VDALLAELST RLGLARGICL 

        70         80         90        100        110        120 
VAVGGYGRGE LFPGSDVDVM LLLPAEPLEA ERQALESWVQ ACWDVGLEIG HSVRTVDACL 

       130        140        150        160        170        180 
AEADADITVE TNLLEARRVW GATALFDDFG RRFRARFDAQ RFFDGKLAEQ HARHARFDDS 

       190        200        210        220        230        240 
AYKLEPNLKD SPGGLRDLHT IHWLAQACDI DAGWSGIARA GLLTEGEARR VAREERWLAK 

       250        260        270        280        290        300 
LRIHLHLLAG RREDRLAFDY QSELAACLGL APTAHRRAGE RLMQGYFRAA KLVQRANDIL 

       310        320        330        340        350        360 
IQSLRVRLFP VVAPPLPIDD DFQLRAGLLE ARDPDVFLRK PDALLRAFLV YARHPQLAGF 

       370        380        390        400        410        420 
EPTTLRAVWR ASARVDRAFR ATPAHRALFI ALLREPLGVT RALRAMHRYG LLGRYIPAFG 

       430        440        450        460        470        480 
RIVGQMQHDL FHVYTVDEHI LTVLRNLRRF TVAQLAHEFP LASRLIAAFD KPELLYLAAL 

       490        500        510        520        530        540 
FHDIAKGRGG DHSALGALDA RGFCRQHGLD KTDTDLVAWL VDMHLVMSRT SQKEDISDPK 

       550        560        570        580        590        600 
VIAAFAARVG DTRRLDALYL LTVADIRGTS PTVWNAWKGK LLEDLYHAAF ARLQGADLAI 

       610        620        630        640        650        660 
AGIAARREEA RVNLALYGLP RDAADALWRH LDKAYFARFD ARDMAWHARM LWRRDATAGA 

       670        680        690        700        710        720 
VVRARLSPAG EGIQVMVYAP DRPDIFVRIC AFFARIQYTV LEAKIHTTRN GYALDSFQVM 

       730        740        750        760        770        780 
DLAHRNIHYR DFLAFVEYEL ARDLDPARPL QAVQPGRLSR HQRHHPYPAA VHLEADRGGD 

       790        800        810        820        830        840 
GQVLSITCAD RGGLLFAIAE ELMRHEISVY AAKIDTLGER VEDTFLIRGE RLNAPPERAA 

       850 
LENELRGVLG 

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References

[1]"The genome sequence of the obligately chemolithoautotrophic, facultatively anaerobic bacterium Thiobacillus denitrificans."
Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W., Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.
J. Bacteriol. 188:1473-1488(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25259.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000116 Genomic DNA. Translation: AAZ96736.1.
RefSeqYP_314541.1. NC_007404.1.

3D structure databases

ProteinModelPortalQ3SKP1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING292415.Tbd_0783.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ96736; AAZ96736; Tbd_0783.
GeneID3673977.
KEGGtbd:Tbd_0783.
PATRIC23967735. VBIThiDen82923_0782.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycTDEN292415:GHWG-804-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]
PfamPF08335. 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_THIDA
AccessionPrimary (citable) accession number: Q3SKP1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 11, 2005
Last modified: June 11, 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