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Q1QRM1

- GLND_NITHX

UniProt

Q1QRM1 - GLND_NITHX

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, Nham_0226
Organism
Nitrobacter hamburgensis (strain X14 / DSM 10229)
Status
Reviewed - Annotation score: 4 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

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

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. metal ion binding Source: InterPro
  4. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. nitrogen compound metabolic process Source: InterPro
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
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 enzyme
Short name:
UTase/UR
Alternative name(s):
Bifunctional [protein-PII] modification enzyme
Bifunctional nitrogen sensor protein
Including the following 2 domains:
[Protein-PII] uridylyltransferase (EC:2.7.7.59)
Short name:
PII uridylyltransferase
Short name:
UTase
[Protein-PII]-UMP uridylyl-removing enzyme (EC:3.1.4.-)
Short name:
UR
Gene namesi
Name:glnD
Ordered Locus Names:Nham_0226
OrganismiNitrobacter hamburgensis (strain X14 / DSM 10229)
Taxonomic identifieri323097 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter
ProteomesiUP000001953: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 931931Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_1000022348Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi323097.Nham_0226.

Structurei

3D structure databases

ProteinModelPortaliQ1QRM1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini500 – 59798HD
Add
BLAST
Domaini740 – 82283ACT 1
Add
BLAST
Domaini851 – 93181ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 383383UridylyltransferaseUniRule annotation
Add
BLAST
Regioni384 – 739356Uridylyl-removingUniRule annotation
Add
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 By similarity.UniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261779.
KOiK00990.
OMAiLYCLWDM.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[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

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MDLATTNDAA GAGNDFDTAR ITGDIDALAA KHAGHEDVFR AAVSRLLKAE    50
LAKVRDAAQA KLLRDRHGRR CAERLCFIQD EIIRLSFSAA TRHLYHSPIP 100
SDGERMAVVA TGGYGRGLMA PESDIDLLFI LPYKQTAWGE QVAEAILYCL 150
WDMGLNVGHA TRSVNESIRQ ARRDMTVRTG ILETRFLAGD RALYDELVTR 200
FDTEVVQGTA AEFVTAKLAE REERHRRAGQ SRYLVEPNVK DGKGGLRDLH 250
TLFWIAKYVY RVHESRELLG CGVFDVREYR TFRRCADFLW SVRCNLHFAT 300
GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLT AKDVGDLTAI 350
LCAKLEDQQA KPAPVLGRMM SRRRPGTELR RVPEGDDFII DNNRINLAAP 400
DVFKRDPVNL IRVFRLAQKN NLAFHPDALR TVTRSRRLIN AQLRENPEAN 450
RLFMEILTSN DAETVLRRMN ETGVLGHFIR AFGKIVSMMQ FNMYHHYTVD 500
EHLLRCIGIL QDIERGGNDE LALASELMRK IHPEHRPVIY ITTLLHDIAK 550
GRPEDHSIAG ARVARRLCPR LGFNASDTEL IAWLIEQHLT MSKVAQSRDL 600
SDRKTIENFA AVVQSVEQMK LLTILTTADI RGVGPGVWNG WKAQLLRTLY 650
YETEPVLTGG FSEVNRVQRI AEAQAEFRAA FTEWSEPELN AYIARHYPAY 700
WLKVDLAHKI RHARFLRASE QGGRKLNINV GFDEARGVTE LTIFAADHPW 750
LLSIIAGACA SAGANIVDAQ IYTTTDGQAL DTIAISREYD RDEDEGRRAA 800
RIGEIIEQVI DGRLRLPDVV ARRAAGKTRL RPFVVEPKVI VNNQWSDRHT 850
VIEVSGLDRP GLLFQLTAAI SKLNLNIASA HVATFGERAR DVFYVTDLLG 900
ARITAPTRQA AIKRALIHLL ANGGAAEQSV G 931
Length:931
Mass (Da):104,795
Last modified:May 16, 2006 - v1
Checksum:i4609DB25262D4648
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
GeneIDi4030820.
KEGGinha:Nham_0226.
PATRICi22687799. VBINitHam61822_0939.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000319 Genomic DNA. Translation: ABE61126.1 .
RefSeqi WP_011508832.1. NC_007964.1.
YP_575586.1. NC_007964.1.

3D structure databases

ProteinModelPortali Q1QRM1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 323097.Nham_0226.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABE61126 ; ABE61126 ; Nham_0226 .
GeneIDi 4030820.
KEGGi nha:Nham_0226.
PATRICi 22687799. VBINitHam61822_0939.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261779.
KOi K00990.
OMAi LYCLWDM.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci NHAM323097:GHP7-230-MONOMER.

Family and domain databases

Gene3Di 1.10.3210.10. 1 hit.
HAMAPi MF_00277. PII_uridylyl_transf.
InterProi IPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF006288. PII_uridyltransf. 1 hit.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01693. UTase_glnD. 1 hit.
PROSITEi PS51671. ACT. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 61 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

External Data

Dasty 3

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