Skip Header

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

Q2NRK5

- GLND_SODGM

UniProt

Q2NRK5 - GLND_SODGM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Sodalis glossinidius (strain morsitans)
Status
Reviewed - 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

Magnesium.UniRule annotation

Enzyme regulationi

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

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. 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 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: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 enzymePRO_1000204801Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi343509.SG1945.

Structurei

3D structure databases

ProteinModelPortaliQ2NRK5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini474 – 607134HDUniRule annotationAdd
BLAST
Domaini715 – 79682ACT 1UniRule annotationAdd
BLAST
Domaini822 – 89675ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 355355UridylyltransferaseAdd
BLAST
Regioni356 – 714359Uridylyl-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.
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

« Hide

        10         20         30         40         50
MQGDPMPDQI LQFTHPPVPR QPPVKPSSPL TWPDDALNRP FLKERLDEFQ
60 70 80 90 100
RWLADAFDAG ETAEILVDAR TLYIDQLLRQ LWHYHGLAHA PHTALVAVGG
110 120 130 140 150
YGRGELHPLS DIDVLVLSQA PLTPPQQQHI SELLTLLWDL KLEVGHSVRS
160 170 180 190 200
IAECLEEGRA DLTVATNLIE SRLICGDLAL FLTLQKQVFS DDFWPSRAFF
210 220 230 240 250
PAKLAEQQER HSRYHGTSYN LEPDIKSSPG GLRDIHTLLW VAHRHFGATS
260 270 280 290 300
MDEMVGFGFI TRAERDELNE CQSFLWRTRF ALHLVLNRYD NRLLFDRQQN
310 320 330 340 350
VAQLLRYQGE GNLPVERMMK DFFRVTRRVS ELNQMLLQLF DEAILALAPD
360 370 380 390 400
EKPQPLDDEF QLRGNLIDLR DETLFSRQPE AILLLFWQMV RNRHIEGIYS
410 420 430 440 450
ATLRQLRYAR RHLKAPLCTS PEARTLFMRI LHQPGAVKHA LLPMHRHSVL
460 470 480 490 500
WAYMPQWSNI VGQMQFDLFH AYTVDEHTIR VLLKLESFAD ESQRPYHPLC
510 520 530 540 550
VELFPRLSQR HLLLVAALFH DIAKGRGGDH SQLGARDVLE FAALHDLPAE
560 570 580 590 600
DAQLVAWLVE SHLVMSVTAQ RRDIQEPDVL VQFAGEMQSE SRLHYLLCLT
610 620 630 640 650
VADICATNET LWNSWKQSLL RELFFATEKQ LRRGIHVSPD VRERVRHNRR
660 670 680 690 700
QSLVLLRMEG IDEQRLQEIW SRCRADYFLR HTPNQLAWHA RHMVLHDHDE
710 720 730 740 750
PLVLISPQAT RGGTEIFIHN QDRPYLFAAV TGELDRRNLS VHDAQIFTNR
760 770 780 790 800
DGMAMDTFVV LEPDGSPLSP DRHPVIRQAL LQILLPGDYR HPRVRRPSSK
810 820 830 840 850
LRHFNVDTSV VFLPSPTERR SYLELTALDQ PGLLARVSEV FVDLGISLHG
860 870 880 890
ARISTIGERV EDLFILADGD RRALSRAMQA EVRRRLTEAL NPNDKV
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: October 29, 2014
This is version 71 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