Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9RAE4 (GLND_RHILV) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismRhizobium leguminosarum bv. viciae
Taxonomic identifier387 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length944 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, 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 likely 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 metabolism. Ref.1

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP-Rule MF_00277

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. HAMAP-Rule MF_00277

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00277

Enzyme regulation

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine likely activates uridylyl-removing (UR) activity. Ref.1

Induction

Is constitutively expressed, irrespective of the nitrogen content of the medium. Ref.1

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

Disruption phenotype

Deletions in the 5'-region of this gene appear to be lethal. Insertion mutations in the central part of this gene abolishes the ability to use nitrate as a sole nitrogen source but not glutamine. In addition, neither uridylylation of PII nor induction of the ntr-regulated glnII gene (encoding glutamine synthetase II) under ammonium deficiency can be observed in mutant strains. Ref.1

Sequence similarities

Belongs to the GlnD family.

Contains 2 ACT domains.

Contains 1 HD domain.

Sequence caution

The sequence AAF17352.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 944944Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192758

Regions

Domain488 – 602115HD
Domain728 – 80982ACT 1
Domain839 – 91880ACT 2
Region1 – 371371Uridylyltransferase HAMAP-Rule MF_00277
Region372 – 727356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q9RAE4 [UniParc].

Last modified December 8, 2000. Version 2.
Checksum: B164E74FF9E6DF2E

FASTA944106,218
        10         20         30         40         50         60 
MRDLDFTNIL DVELLQKQCD AVAEANRNRP DVLRADLLAV LKKASTEGRQ KAREALMADG 

        70         80         90        100        110        120 
GGLNCAYRIS WLQDQITTVL YNFATAHIFP QQKDKFAVTA VGGYGRDTLA PGSDIDLLFL 

       130        140        150        160        170        180 
FLPRPAEETH KAVEFMLYVL WDMGFKVGHA TRTVEECIAL SKSDMTIRTA ILEMRYICGL 

       190        200        210        220        230        240 
QRLETELETR FDKEIVTGTG PEFIAAKLAE RDERHRKAGD TRYLVEPNVK EGKGGLRDLH 

       250        260        270        280        290        300 
TLFWISKYYY HVRDQAELVK LGVLSKHEYR LLEKADDFLW AVRCHMHFLT GKAEERLSFD 

       310        320        330        340        350        360 
IQREIAEAFG YHTRPGLSAV ERFMKHYFLV AKDVGDLTRI LCAALEDQQA KSIPGLTGVI 

       370        380        390        400        410        420 
SRFTHRNRKI AGSVEFVEDR GRIALADPEV FKRDPVNIIR LFHVADINGL EFHPDALKRV 

       430        440        450        460        470        480 
TRSLALIDNA LRENDEANRL FMSILTSKRD PALILRRMNE AGVLGRFIPE FGKIVAMMQF 

       490        500        510        520        530        540 
NMYHHYTVDE HLIRTVDILS EIDKGRAEDL HPLANKLMPG IEDREALYVA VLLHDIAKGR 

       550        560        570        580        590        600 
QEDHSIAGAR VARKLCVRFG LSQKQTEIVV WLIEEHLTMS MVAQTRDLTD RKTITDFADR 

       610        620        630        640        650        660 
VQSLDRLKML LILTICDIRA VGPGVWNGWK GQLLRTLYYE TELLLAGGFS EVSRKERANA 

       670        680        690        700        710        720 
AAEALHSALA DWSQKDRNTY TKLHYQPYLL SVPLEDQIRH AHFIRQADKA GQALATMVRT 

       730        740        750        760        770        780 
DSFHAITEIT VLSPDHPRLL AVIAGACAAA GANIVDAQIF TTSDGRALDT IHVSREFTDD 

       790        800        810        820        830        840 
ADELRRAATI GRMIEDVLSG RKRLPEVIAT RARNRKKSKA FVIPPSVNIT NSLSNKFTVI 

       850        860        870        880        890        900 
EVECLDRPGL LSEITAVLSD LSLDIQSARI TTFGEKVIDT FYVTDLVGQK ISGDSKRANI 

       910        920        930        940 
TARMKAVMAE EEDELRERMP SGIIAPAATA RTPPASEKKA GSPI 

« Hide

References

[1]"The Rhizobium leguminosarum bv. viciae glnD gene, encoding a uridylyltransferase/uridylyl-removing enzyme, is expressed in the root nodule but is not essential for nitrogen fixation."
Schluter A., Nohlen M., Kramer M., Defez R., Priefer U.B.
Microbiology 146:2987-2996(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ENZYME REGULATION, INDUCTION, DISRUPTION PHENOTYPE.
Strain: VF39.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF155830 Genomic DNA. Translation: AAF17352.1. Different initiation.

3D structure databases

ProteinModelPortalQ9RAE4.
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]
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_RHILV
AccessionPrimary (citable) accession number: Q9RAE4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: December 8, 2000
Last modified: June 11, 2014
This is version 67 of the entry and version 2 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