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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Brucella melitensis biotype 2 (strain ATCC 23457)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
Short name:
UTase/URUniRule annotation
Alternative name(s):
Bifunctional [protein-PII] modification enzymeUniRule annotation
Bifunctional nitrogen sensor proteinUniRule annotation
Including the following 2 domains:
[Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
Short name:
PII uridylyltransferaseUniRule annotation
Short name:
UTaseUniRule annotation
[Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
Short name:
URUniRule annotation
Gene namesi
Name:glnDUniRule annotation
Ordered Locus Names:BMEA_A0150
OrganismiBrucella melitensis biotype 2 (strain ATCC 23457)
Taxonomic identifieri546272 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000001748 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001325261 – 934Bifunctional uridylyltransferase/uridylyl-removing enzymeAdd BLAST934

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini497 – 613HDUniRule annotationAdd BLAST117
Domaini737 – 818ACT 1UniRule annotationAdd BLAST82
Domaini848 – 931ACT 2UniRule annotationAdd BLAST84

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 379UridylyltransferaseAdd BLAST379
Regioni380 – 736Uridylyl-removingAdd BLAST357

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the GlnD family.UniRule annotation
Contains 2 ACT domains.UniRule annotation
Contains 1 HD domain.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000261779.
KOiK00990.
OMAiARICGYF.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf. 1 hit.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
[Graphical view]
PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

C0RGK0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAHDLKLEE IVNAETLRRK LNELADTADE SYTSLPMRKV VLQTLKDALA
60 70 80 90 100
SGRANAEDML MKDGGGTLCA KRLCYLMDTL IDILFEFATT RAYPTRNPSK
110 120 130 140 150
AENMALVAVG GYGRGGLAQG SDIDLLFLLP YKQTPWGEQV VEHTLYMLWD
160 170 180 190 200
MGLKVGHSTR NIDECIRLAR EDMTIRTALL DARFLTGDKD LFRTLEIRFE
210 220 230 240 250
EEIVKGTEPE FIQAKLAERD ARHRKAGETR YLVEPNVKEG KGGQRDLHTL
260 270 280 290 300
FWITKYFYRV KTKEELVKLG VLSRAELKLF NKAEDFLWAV RCHMHFATLK
310 320 330 340 350
AEERLSFDIQ PEIAQRLGYT AHPGQNYVER FMKHYFLVAK DVGDLTRIIC
360 370 380 390 400
AALEEQQAKH VPGFNRIFLT FSRRKRKLSD DGAFISENHR INIARPDIFR
410 420 430 440 450
QDPVNMIRLF HLADRHGLEF HPEAMQSLTR SLKLINADLR ENPEANRLFL
460 470 480 490 500
EILTSPRNPE LILRRMNESG VLGKFIPDFG KIVAMMQFNM YHHYTVDEHL
510 520 530 540 550
LRCIAVLSEI EHGELKTEHP LSNHLITTIK RDRNLLYVTL LLHDIAKGRP
560 570 580 590 600
EDHSIAGARI ARRLCPRFGL TPSETETVEW LVREHLTMSM VAQSRDLNDR
610 620 630 640 650
KTIIDFADTV QTMERLKLLL ILTVCDIKAV GPGIWNGWKG QLLRTLFYET
660 670 680 690 700
ELVLTGGFSE LSRAARDKQA REALAERLSD WPKEERDAYL ALPYTNYFLT
710 720 730 740 750
VSLDDQVRHA HFIRDADQQG RALVTMAKPH AFEAVTEITV LAPDHPRLLS
760 770 780 790 800
VITGACAAAG GNIVDAQIFT TSDGRALDTI LISREFDTDD DERRRAERVG
810 820 830 840 850
KVIEDVLSGK AHLPDMLAKR TKPKKAARAF KVEPRVEINN TLSNKFTVIE
860 870 880 890 900
VEGLDRPGLL SELTGLISDL SLDIASAHIT TFGEKVIDSF YVTDLVGHKI
910 920 930
SNATRQGNIK RKLLALLGAE NGARTNGRSP QAAA
Length:934
Mass (Da):105,904
Last modified:May 5, 2009 - v1
Checksum:iC4F873C09366CF25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001488 Genomic DNA. Translation: ACN99957.1.
RefSeqiWP_004686653.1. NC_012441.1.

Genome annotation databases

EnsemblBacteriaiACN99957; ACN99957; BMEA_A0150.
KEGGibmi:BMEA_A0150.
PATRICi17835987. VBIBruMel14466_0158.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001488 Genomic DNA. Translation: ACN99957.1.
RefSeqiWP_004686653.1. NC_012441.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACN99957; ACN99957; BMEA_A0150.
KEGGibmi:BMEA_A0150.
PATRICi17835987. VBIBruMel14466_0158.

Phylogenomic databases

HOGENOMiHOG000261779.
KOiK00990.
OMAiARICGYF.

Miscellaneous databases

PROiC0RGK0.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf. 1 hit.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
[Graphical view]
PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGLND_BRUMB
AccessioniPrimary (citable) accession number: C0RGK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: November 2, 2016
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.