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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 Publication
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].1 Publication

Cofactori

Magnesium By similarity.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 Publication

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 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 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
OrganismiAzospirillum brasilense
Taxonomic identifieri192 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 933933Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_0000192716Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ8RQD1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini507 – 637131HDAdd
BLAST
Domaini746 – 82984ACT 1Add
BLAST
Domaini859 – 93375ACT 2Add
BLAST

Region

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

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

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MLSTRAASAD ASDAKDAGTA NIPNKRAILS RRKLAEDLET LVAEHGTGDK    50
LRPALIARLR GALNDGRAEV RARFEAKGSG EDCVRQNCYL ADGVVRSLAD 100
LTVTHIFPTP NPTSGEVFDI VATGGYGRGE LAPFSDIDLL FLLPYKRTPR 150
VEQVVEYMLY ILWDLGLKVG HAVRSVDDCI RQSKADVTIR TAILESRYLW 200
GPRKLFHRLR RRFDREVVAG TGPEFVEAKL AERDNRHLKL GDSAYVLEPN 250
LKDGKGGLRD LQTLFWIAKY LYRVEDVDDL VGKKVLLPEE AHGFAKAQNF 300
LWTARCHLHY LTGRMEDRMT FDVQTSIGNR MGYTDHAGTK GVERFMKHYF 350
LVAKDVGDLT RIFCAALEAE SKRPPKFNIL RLAALARRKD VDGFVVDGER 400
LNVRSDRQFK DEPLDMIRLF HTAQQNDIDI HPNALRAITR SLSVVGPKLR 450
ADPEANRLFL EILTGRKDPE ITLRRMNEAG VLARFIPDFG RVVAQMQYDM 500
YHVYTVDEHT LFALGILHKI EMGELTDELP LSSEVIHKVV SRRALYVAVL 550
LHDIAKGRGG DHSILGARVA EKLCPRLGLT AEETETVAWL VRWHLAMSYT 600
AFKRDLEDDK TVRDFVSLVQ SPERLRLLLV LTVADIRAVG PQRWNNWKAT 650
LLRELYNRSE EVMSGGLSVE GRGRRIQAAQ AALRDELSDF DAADFERHLA 700
LGYPAYWLAF DAETLGRQAR LVRGRLRDER PLTVNTRIDR GRAITEVTIF 750
ATDHHGLFSR LAGALAAAGA DIVDARIFTM TNGMALDVFT VQDAAGGGAF 800
ESGDKLAKLS VMIEKVLSGQ LKPLHDLTKR KAPHASRTRV FHVPPRVLID 850
NNASTTHTVI EVNGRDRPGL LYDLTRALTN LTLQISSAKI STYGEKAIDV 900
FYVKDVFGLK VTHENKLAQI RERLLHALAD PSA 933
Length:933
Mass (Da):104,602
Last modified:June 1, 2002 - v1
Checksum:i35E692E0411BB9E7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF149716 Genomic DNA. Translation: AAL87737.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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: June 11, 2014
This is version 57 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

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