Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Nitrobacter hamburgensis (strain X14 / DSM 10229)
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

Enzyme and pathway databases

BioCyciNHAM323097:GHP7-230-MONOMER.

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:Nham_0226
OrganismiNitrobacter hamburgensis (strain X14 / DSM 10229)
Taxonomic identifieri323097 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
ProteomesiUP000001953 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 931931Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022348Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi323097.Nham_0226.

Structurei

3D structure databases

ProteinModelPortaliQ1QRM1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini500 – 59798HDUniRule annotationAdd
BLAST
Domaini740 – 82283ACT 1UniRule annotationAdd
BLAST
Domaini851 – 93181ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 383383UridylyltransferaseAdd
BLAST
Regioni384 – 739356Uridylyl-removingAdd
BLAST

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

eggNOGiCOG2844.
HOGENOMiHOG000261779.
KOiK00990.
OMAiSTIGERV.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[Graphical view]
PfamiPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 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.

Q1QRM1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLATTNDAA GAGNDFDTAR ITGDIDALAA KHAGHEDVFR AAVSRLLKAE
60 70 80 90 100
LAKVRDAAQA KLLRDRHGRR CAERLCFIQD EIIRLSFSAA TRHLYHSPIP
110 120 130 140 150
SDGERMAVVA TGGYGRGLMA PESDIDLLFI LPYKQTAWGE QVAEAILYCL
160 170 180 190 200
WDMGLNVGHA TRSVNESIRQ ARRDMTVRTG ILETRFLAGD RALYDELVTR
210 220 230 240 250
FDTEVVQGTA AEFVTAKLAE REERHRRAGQ SRYLVEPNVK DGKGGLRDLH
260 270 280 290 300
TLFWIAKYVY RVHESRELLG CGVFDVREYR TFRRCADFLW SVRCNLHFAT
310 320 330 340 350
GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLT AKDVGDLTAI
360 370 380 390 400
LCAKLEDQQA KPAPVLGRMM SRRRPGTELR RVPEGDDFII DNNRINLAAP
410 420 430 440 450
DVFKRDPVNL IRVFRLAQKN NLAFHPDALR TVTRSRRLIN AQLRENPEAN
460 470 480 490 500
RLFMEILTSN DAETVLRRMN ETGVLGHFIR AFGKIVSMMQ FNMYHHYTVD
510 520 530 540 550
EHLLRCIGIL QDIERGGNDE LALASELMRK IHPEHRPVIY ITTLLHDIAK
560 570 580 590 600
GRPEDHSIAG ARVARRLCPR LGFNASDTEL IAWLIEQHLT MSKVAQSRDL
610 620 630 640 650
SDRKTIENFA AVVQSVEQMK LLTILTTADI RGVGPGVWNG WKAQLLRTLY
660 670 680 690 700
YETEPVLTGG FSEVNRVQRI AEAQAEFRAA FTEWSEPELN AYIARHYPAY
710 720 730 740 750
WLKVDLAHKI RHARFLRASE QGGRKLNINV GFDEARGVTE LTIFAADHPW
760 770 780 790 800
LLSIIAGACA SAGANIVDAQ IYTTTDGQAL DTIAISREYD RDEDEGRRAA
810 820 830 840 850
RIGEIIEQVI DGRLRLPDVV ARRAAGKTRL RPFVVEPKVI VNNQWSDRHT
860 870 880 890 900
VIEVSGLDRP GLLFQLTAAI SKLNLNIASA HVATFGERAR DVFYVTDLLG
910 920 930
ARITAPTRQA AIKRALIHLL ANGGAAEQSV G
Length:931
Mass (Da):104,795
Last modified:May 16, 2006 - v1
Checksum:i4609DB25262D4648
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000319 Genomic DNA. Translation: ABE61126.1.
RefSeqiWP_011508832.1. NC_007964.1.
YP_575586.1. NC_007964.1.

Genome annotation databases

EnsemblBacteriaiABE61126; ABE61126; Nham_0226.
KEGGinha:Nham_0226.
PATRICi22687799. VBINitHam61822_0939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000319 Genomic DNA. Translation: ABE61126.1.
RefSeqiWP_011508832.1. NC_007964.1.
YP_575586.1. NC_007964.1.

3D structure databases

ProteinModelPortaliQ1QRM1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi323097.Nham_0226.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABE61126; ABE61126; Nham_0226.
KEGGinha:Nham_0226.
PATRICi22687799. VBINitHam61822_0939.

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261779.
KOiK00990.
OMAiSTIGERV.
OrthoDBiEOG6CCH44.

Enzyme and pathway databases

BioCyciNHAM323097:GHP7-230-MONOMER.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[Graphical view]
PfamiPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: X14 / DSM 10229.

Entry informationi

Entry nameiGLND_NITHX
AccessioniPrimary (citable) accession number: Q1QRM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: April 29, 2015
This is version 68 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.