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Q3SWE0 (GLND_NITWN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 61. 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:Nwi_0133
OrganismNitrobacter winogradskyi (strain Nb-255 / ATCC 25391) [Complete proteome] [HAMAP]
Taxonomic identifier323098 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length925 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 – 925925Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231682

Regions

Domain500 – 59697HD
Domain739 – 82082ACT 1
Domain849 – 92577ACT 2
Region1 – 382382Uridylyltransferase HAMAP-Rule MF_00277
Region383 – 738356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q3SWE0 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 9B4D8076280C0070

FASTA925104,377
        10         20         30         40         50         60 
MVLPTTKDAT AAGAGFDTVR IIGDIDALAE KHAGHEDVFR SAVSRLLKAE LAKVRDAAQA 

        70         80         90        100        110        120 
KLLRDRHGRH CAEWLCFVQD EIIRLSFSAA TRHLYHSPIP SDGERMAVVA TGGYGRGLMA 

       130        140        150        160        170        180 
PESDIDLLFI LPYKQTAWGE QVAEAILYCL WDMGLNVGHA TRSVNESIRQ ARRDMTVRTG 

       190        200        210        220        230        240 
ILEARFLTGD RALYDELISR FDTEVVQGTA AEFVAAKLAE REERHHRAGQ SRYLVEPNVK 

       250        260        270        280        290        300 
DGKGGLRDLH TLFWIAKYVY RVRESHELLR RNVFDVREYR TFRRCADFLW SVRCNLHFAT 

       310        320        330        340        350        360 
GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLT AKDVGDLTAI LCAKLEDQQA 

       370        380        390        400        410        420 
KPAPVLSRAM SKPPGAEVRR VPDSDDFIID NNRINLAAPD LFKRDPVNLI RLFRLAQKNN 

       430        440        450        460        470        480 
LAFHPDALRM VRRSRRLINA QLREDPESNR LFIEILTSND AETVLRRMNE TGVLGEFIRA 

       490        500        510        520        530        540 
FGKIVSMMQF NMYHHYTVDE HLIRCIGILQ DIERGDNDEV ALAGELMRTI NPEHRPVIYI 

       550        560        570        580        590        600 
ATLLHDVAKG RPEDHSIAGA RVARRLCPRL GFNAADTELV AWLIEQHLTM SKVAQSRDLS 

       610        620        630        640        650        660 
DRKTIENFAA VVQSVERMKL LTILTTADIR GVGPGVWNGW KAQLLRTLYY ETEPVLTGGF 

       670        680        690        700        710        720 
SEVNRAQRMA AAEAEFRAAF TEWSGHELNA YIARHYPAYW LKVDLEHKIR HARFLRASEQ 

       730        740        750        760        770        780 
SGRKLNINVG FDEARGVTEL TILAADHPWL LSIIAGACAS AGANIVDAQI YTTTDGQALD 

       790        800        810        820        830        840 
TIAISREYER DEDEGRRAAR IAEIIEQVLE GRLRLPDVMP SRAAGKRLRP FVVEPKVTIN 

       850        860        870        880        890        900 
NQWSDRHTMI EVSGLDRPGL LFQLTTAISK LNLNIASAHV ATFGERARDV FYVTDLLGAR 

       910        920 
ITAPTRQAAI KRALVHLLAS GNTAE 

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References

[1]"Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium Nitrobacter winogradskyi Nb-255."
Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L., Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., Hickey W.J.
Appl. Environ. Microbiol. 72:2050-2063(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nb-255 / ATCC 25391.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000115 Genomic DNA. Translation: ABA03401.1.
RefSeqYP_316753.1. NC_007406.1.

3D structure databases

ProteinModelPortalQ3SWE0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323098.Nwi_0133.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA03401; ABA03401; Nwi_0133.
GeneID3676202.
KEGGnwi:Nwi_0133.
PATRIC22696587. VBINitWin102302_0149.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycNWIN323098:GJEG-134-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. 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_NITWN
AccessionPrimary (citable) accession number: Q3SWE0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 11, 2005
Last modified: June 11, 2014
This is version 61 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