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Q2NRK5

- GLND_SODGM

UniProt

Q2NRK5 - GLND_SODGM

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, SG1945
Organism
Sodalis glossinidius (strain morsitans)
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

BioCyciSGLO343509:GJJC-2011-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:SG1945
OrganismiSodalis glossinidius (strain morsitans)
Taxonomic identifieri343509 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSodalis
ProteomesiUP000001932: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 896896Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_1000204801Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi343509.SG1945.

Structurei

3D structure databases

ProteinModelPortaliQ2NRK5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini474 – 607134HD
Add
BLAST
Domaini715 – 79682ACT 1
Add
BLAST
Domaini822 – 89675ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 355355UridylyltransferaseUniRule annotation
Add
BLAST
Regioni356 – 714359Uridylyl-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.
KOiK00990.
OMAiHHLLMSV.
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.

Q2NRK5-1 [UniParc]FASTAAdd to Basket

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MQGDPMPDQI LQFTHPPVPR QPPVKPSSPL TWPDDALNRP FLKERLDEFQ    50
RWLADAFDAG ETAEILVDAR TLYIDQLLRQ LWHYHGLAHA PHTALVAVGG 100
YGRGELHPLS DIDVLVLSQA PLTPPQQQHI SELLTLLWDL KLEVGHSVRS 150
IAECLEEGRA DLTVATNLIE SRLICGDLAL FLTLQKQVFS DDFWPSRAFF 200
PAKLAEQQER HSRYHGTSYN LEPDIKSSPG GLRDIHTLLW VAHRHFGATS 250
MDEMVGFGFI TRAERDELNE CQSFLWRTRF ALHLVLNRYD NRLLFDRQQN 300
VAQLLRYQGE GNLPVERMMK DFFRVTRRVS ELNQMLLQLF DEAILALAPD 350
EKPQPLDDEF QLRGNLIDLR DETLFSRQPE AILLLFWQMV RNRHIEGIYS 400
ATLRQLRYAR RHLKAPLCTS PEARTLFMRI LHQPGAVKHA LLPMHRHSVL 450
WAYMPQWSNI VGQMQFDLFH AYTVDEHTIR VLLKLESFAD ESQRPYHPLC 500
VELFPRLSQR HLLLVAALFH DIAKGRGGDH SQLGARDVLE FAALHDLPAE 550
DAQLVAWLVE SHLVMSVTAQ RRDIQEPDVL VQFAGEMQSE SRLHYLLCLT 600
VADICATNET LWNSWKQSLL RELFFATEKQ LRRGIHVSPD VRERVRHNRR 650
QSLVLLRMEG IDEQRLQEIW SRCRADYFLR HTPNQLAWHA RHMVLHDHDE 700
PLVLISPQAT RGGTEIFIHN QDRPYLFAAV TGELDRRNLS VHDAQIFTNR 750
DGMAMDTFVV LEPDGSPLSP DRHPVIRQAL LQILLPGDYR HPRVRRPSSK 800
LRHFNVDTSV VFLPSPTERR SYLELTALDQ PGLLARVSEV FVDLGISLHG 850
ARISTIGERV EDLFILADGD RRALSRAMQA EVRRRLTEAL NPNDKV 896
Length:896
Mass (Da):103,328
Last modified:February 7, 2006 - v1
Checksum:i2BAC301F1C44FF4D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008232 Genomic DNA. Translation: BAE75220.1.
RefSeqiYP_455625.1. NC_007712.1.

Genome annotation databases

EnsemblBacteriaiBAE75220; BAE75220; SG1945.
GeneIDi3867857.
KEGGisgl:SG1945.
PATRICi23654843. VBISodGlo61428_4706.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AP008232 Genomic DNA. Translation: BAE75220.1 .
RefSeqi YP_455625.1. NC_007712.1.

3D structure databases

ProteinModelPortali Q2NRK5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 343509.SG1945.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE75220 ; BAE75220 ; SG1945 .
GeneIDi 3867857.
KEGGi sgl:SG1945.
PATRICi 23654843. VBISodGlo61428_4706.

Phylogenomic databases

eggNOGi COG2844.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci SGLO343509:GJJC-2011-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. "Massive genome erosion and functional adaptations provide insights into the symbiotic lifestyle of Sodalis glossinidius in the tsetse host."
    Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M., Aksoy S.
    Genome Res. 16:149-156(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: morsitans.

Entry informationi

Entry nameiGLND_SODGM
AccessioniPrimary (citable) accession number: Q2NRK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 7, 2006
Last modified: June 11, 2014
This is version 69 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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