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Q8RQD1 (GLND_AZOBR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:

  1. [Protein-PII] uridylyltransferase
    Short name=PII uridylyltransferase
    Short name=UTase
    EC=2.7.7.59
  2. [Protein-PII]-UMP uridylyl-removing enzyme
    Short name=UR
    EC=3.1.4.-
Gene names
Name:glnD
OrganismAzospirillum brasilense
Taxonomic identifier192 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeAzospirillum

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. Ref.2

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. Ref.2

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00277

Enzyme regulation

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. Ref.2

Domain

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. HAMAP-Rule MF_00277

Sequence similarities

Belongs to the GlnD family.

Contains 2 ACT domains.

Contains 1 HD domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 933933Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192716

Regions

Domain507 – 637131HD
Domain746 – 82984ACT 1
Domain859 – 93375ACT 2
Region1 – 390390Uridylyltransferase HAMAP-Rule MF_00277
Region391 – 745355Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q8RQD1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 35E692E0411BB9E7

FASTA933104,602
        10         20         30         40         50         60 
MLSTRAASAD ASDAKDAGTA NIPNKRAILS RRKLAEDLET LVAEHGTGDK LRPALIARLR 

        70         80         90        100        110        120 
GALNDGRAEV RARFEAKGSG EDCVRQNCYL ADGVVRSLAD LTVTHIFPTP NPTSGEVFDI 

       130        140        150        160        170        180 
VATGGYGRGE LAPFSDIDLL FLLPYKRTPR VEQVVEYMLY ILWDLGLKVG HAVRSVDDCI 

       190        200        210        220        230        240 
RQSKADVTIR TAILESRYLW GPRKLFHRLR RRFDREVVAG TGPEFVEAKL AERDNRHLKL 

       250        260        270        280        290        300 
GDSAYVLEPN LKDGKGGLRD LQTLFWIAKY LYRVEDVDDL VGKKVLLPEE AHGFAKAQNF 

       310        320        330        340        350        360 
LWTARCHLHY LTGRMEDRMT FDVQTSIGNR MGYTDHAGTK GVERFMKHYF LVAKDVGDLT 

       370        380        390        400        410        420 
RIFCAALEAE SKRPPKFNIL RLAALARRKD VDGFVVDGER LNVRSDRQFK DEPLDMIRLF 

       430        440        450        460        470        480 
HTAQQNDIDI HPNALRAITR SLSVVGPKLR ADPEANRLFL EILTGRKDPE ITLRRMNEAG 

       490        500        510        520        530        540 
VLARFIPDFG RVVAQMQYDM YHVYTVDEHT LFALGILHKI EMGELTDELP LSSEVIHKVV 

       550        560        570        580        590        600 
SRRALYVAVL LHDIAKGRGG DHSILGARVA EKLCPRLGLT AEETETVAWL VRWHLAMSYT 

       610        620        630        640        650        660 
AFKRDLEDDK TVRDFVSLVQ SPERLRLLLV LTVADIRAVG PQRWNNWKAT LLRELYNRSE 

       670        680        690        700        710        720 
EVMSGGLSVE GRGRRIQAAQ AALRDELSDF DAADFERHLA LGYPAYWLAF DAETLGRQAR 

       730        740        750        760        770        780 
LVRGRLRDER PLTVNTRIDR GRAITEVTIF ATDHHGLFSR LAGALAAAGA DIVDARIFTM 

       790        800        810        820        830        840 
TNGMALDVFT VQDAAGGGAF ESGDKLAKLS VMIEKVLSGQ LKPLHDLTKR KAPHASRTRV 

       850        860        870        880        890        900 
FHVPPRVLID NNASTTHTVI EVNGRDRPGL LYDLTRALTN LTLQISSAKI STYGEKAIDV 

       910        920        930 
FYVKDVFGLK VTHENKLAQI RERLLHALAD PSA 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF149716 Genomic DNA. Translation: AAL87737.1.

3D structure databases

ProteinModelPortalQ8RQD1.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFPIRSF006288. PII_uridyltransf. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR01693. UTase_glnD. 1 hit.
PROSITEPS51671. ACT. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLND_AZOBR
AccessionPrimary (citable) accession number: Q8RQD1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: June 1, 2002
Last modified: February 19, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families