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Q8RQD1

- GLND_AZOBR

UniProt

Q8RQD1 - GLND_AZOBR

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Azospirillum brasilense
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnZ, 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 fixation and metabolism.1 Publication

Catalytic activityi

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].1 PublicationUniRule annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].1 PublicationUniRule annotation

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity. Uridylylation process is dependent on ATP and 2-oxoglutarate, which are effector molecules that likely bind to PII proteins and control their activity.1 PublicationUniRule 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 fixation Source: UniProtKB-KW
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Biological processi

Nitrogen fixation

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
OrganismiAzospirillum brasilense
Taxonomic identifieri192 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 933933Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192716Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ8RQD1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini507 – 637131HDUniRule annotationAdd
BLAST
Domaini746 – 82984ACT 1UniRule annotationAdd
BLAST
Domaini859 – 93375ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 390390UridylyltransferaseAdd
BLAST
Regioni391 – 745355Uridylyl-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

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.

Q8RQD1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSTRAASAD ASDAKDAGTA NIPNKRAILS RRKLAEDLET LVAEHGTGDK
60 70 80 90 100
LRPALIARLR GALNDGRAEV RARFEAKGSG EDCVRQNCYL ADGVVRSLAD
110 120 130 140 150
LTVTHIFPTP NPTSGEVFDI VATGGYGRGE LAPFSDIDLL FLLPYKRTPR
160 170 180 190 200
VEQVVEYMLY ILWDLGLKVG HAVRSVDDCI RQSKADVTIR TAILESRYLW
210 220 230 240 250
GPRKLFHRLR RRFDREVVAG TGPEFVEAKL AERDNRHLKL GDSAYVLEPN
260 270 280 290 300
LKDGKGGLRD LQTLFWIAKY LYRVEDVDDL VGKKVLLPEE AHGFAKAQNF
310 320 330 340 350
LWTARCHLHY LTGRMEDRMT FDVQTSIGNR MGYTDHAGTK GVERFMKHYF
360 370 380 390 400
LVAKDVGDLT RIFCAALEAE SKRPPKFNIL RLAALARRKD VDGFVVDGER
410 420 430 440 450
LNVRSDRQFK DEPLDMIRLF HTAQQNDIDI HPNALRAITR SLSVVGPKLR
460 470 480 490 500
ADPEANRLFL EILTGRKDPE ITLRRMNEAG VLARFIPDFG RVVAQMQYDM
510 520 530 540 550
YHVYTVDEHT LFALGILHKI EMGELTDELP LSSEVIHKVV SRRALYVAVL
560 570 580 590 600
LHDIAKGRGG DHSILGARVA EKLCPRLGLT AEETETVAWL VRWHLAMSYT
610 620 630 640 650
AFKRDLEDDK TVRDFVSLVQ SPERLRLLLV LTVADIRAVG PQRWNNWKAT
660 670 680 690 700
LLRELYNRSE EVMSGGLSVE GRGRRIQAAQ AALRDELSDF DAADFERHLA
710 720 730 740 750
LGYPAYWLAF DAETLGRQAR LVRGRLRDER PLTVNTRIDR GRAITEVTIF
760 770 780 790 800
ATDHHGLFSR LAGALAAAGA DIVDARIFTM TNGMALDVFT VQDAAGGGAF
810 820 830 840 850
ESGDKLAKLS VMIEKVLSGQ LKPLHDLTKR KAPHASRTRV FHVPPRVLID
860 870 880 890 900
NNASTTHTVI EVNGRDRPGL LYDLTRALTN LTLQISSAKI STYGEKAIDV
910 920 930
FYVKDVFGLK VTHENKLAQI RERLLHALAD PSA
Length:933
Mass (Da):104,602
Last modified:June 1, 2002 - v1
Checksum:i35E692E0411BB9E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149716 Genomic DNA. Translation: AAL87737.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF149716 Genomic DNA. Translation: AAL87737.1 .

3D structure databases

ProteinModelPortali Q8RQD1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

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. "Cloning and characterization of the Azospirillum brasilense glnD gene and analysis of a glnD mutant."
    Van Dommelen A., Keijers V., Somers E., Vanderleyden J.
    Mol. Gen. Genet. 266:813-820(2002)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 29145 / Sp7 / DSM 1690 / IMET 11303.
  2. "Different responses of the GlnB and GlnZ proteins upon in vitro uridylylation by the Azospirillum brasilense GlnD protein."
    Araujo L.M., Huergo L.F., Invitti A.L., Gimenes C.I., Bonatto A.C., Monteiro R.A., Souza E.M., Pedrosa F.O., Chubatsu L.S.
    Braz. J. Med. Biol. Res. 41:289-294(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
    Strain: FP2.

Entry informationi

Entry nameiGLND_AZOBR
AccessioniPrimary (citable) accession number: Q8RQD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 60 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

Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3