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B2S8D8 (GLND_BRUA1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:BAbS19_I01350
OrganismBrucella abortus (strain S19) [Complete proteome] [HAMAP]
Taxonomic identifier430066 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length934 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 – 934934Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000114750

Regions

Domain497 – 613117HD
Domain737 – 81882ACT 1
Domain848 – 93184ACT 2
Region1 – 379379Uridylyltransferase HAMAP-Rule MF_00277
Region380 – 736357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
B2S8D8 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: 74F9987863AE3BFE

FASTA934105,930
        10         20         30         40         50         60 
MSAHDLKLEE IVNAETLRRK LNELADTADE SYTSLPMRKV VLQTLKDALA SGRANAEDML 

        70         80         90        100        110        120 
MKDGGGTLCA KRLCYLMDTL IDILFEFATT RAYPTRNPSK AENMALVAVG GYGRGGLAQG 

       130        140        150        160        170        180 
SDIDLLFLLP YKQTPWGEQV VEYTLYMLWD MGLKVGHSTR NIDECIRLAR EDMTIRTALL 

       190        200        210        220        230        240 
DARFLTGDKD LFRTLEIRFE EEIVKGTEPE FIQAKLAERD ARHRKAGETR YLVEPNVKEG 

       250        260        270        280        290        300 
KGGQRDLHTL FWITKYFYRV KTKEELVKLG VLSRAELKLF NKAEDFLWAV RCHMHFATLK 

       310        320        330        340        350        360 
AEERLSFDIQ PEIAQRLGYT AHPGQNYVER FMKHYFLVAK DVGDLTRIIC AALEEQQAKH 

       370        380        390        400        410        420 
VPGFNRIFLT FSRRKRKLSD DGAFISENHR INIARPDIFR QDPVNMIRLF HLADRHGLEF 

       430        440        450        460        470        480 
HPEAMQSLTR SLKLINADLR ENPEANRLFL EILTSPRNPE LILRRMNESG VLGKFIPDFG 

       490        500        510        520        530        540 
KIVAMMQFNM YHHYTVDEHL LRCIAVLSEI EHGELKTEHP LSNHLITTIK RDRNLLYVTL 

       550        560        570        580        590        600 
LLHDIAKGRP EDHSIAGARI ARRLCPRFGL TPSETETVEW LVREHLTMSM VAQSRDLNDR 

       610        620        630        640        650        660 
KTIIDFADTV QTMERLKLLL ILTVCDIKAV GPGIWNGWKG QLLRTLFYET ELVLTGGFSE 

       670        680        690        700        710        720 
LSRAARDKQA REALAERLSD WPKEERDAYL ALPYTNYFLT VSLDDQVRHA HFIRDADQQG 

       730        740        750        760        770        780 
RALVTMAKPH AFEAVTEITV LAPDHPRLLS VITGACAAAG GNIVDAQIFT TSDGRALDTI 

       790        800        810        820        830        840 
LISREFDTDD DERRRAERVG KVIEDVLSGK AHLPDMLAKR TKPKKAARAF KVEPRVEINN 

       850        860        870        880        890        900 
TLSNKFTVIE VEGLDRPGLL SELTGLISDL SLDIASAHIT TFGEKVIDSF YVTDLVGHKI 

       910        920        930 
SNATRQGNIK RKLLALLGAE NGARTNGRSP QAAA 

« Hide

References

[1]"Genome sequence of Brucella abortus vaccine strain S19 compared to virulent strains yields candidate virulence genes."
Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.
PLoS ONE 3:E2193-E2193(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: S19.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000887 Genomic DNA. Translation: ACD71691.1.
RefSeqYP_001934165.1. NC_010742.1.

3D structure databases

ProteinModelPortalB2S8D8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING430066.BAbS19_I01350.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD71691; ACD71691; BAbS19_I01350.
GeneID6328081.
KEGGbmc:BAbS19_I01350.
PATRIC17817143. VBIBruAbo38055_1354.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05092.

Enzyme and pathway databases

BioCycBABO430066:GHI6-134-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]
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...

Other

PROB2S8D8.

Entry information

Entry nameGLND_BRUA1
AccessionPrimary (citable) accession number: B2S8D8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 43 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