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Q98C27 (GLND_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 75. 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
Ordered Locus Names:mll5321
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length933 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 fixation and metabolism By similarity. HAMAP-Rule MF_00277

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 activates uridylyl-removing (UR) activity By similarity. HAMAP-Rule MF_00277

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_0000192759

Regions

Domain497 – 596100HD
Domain737 – 81882ACT 1
Domain848 – 92275ACT 2
Region1 – 379379Uridylyltransferase HAMAP-Rule MF_00277
Region380 – 736357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q98C27 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: 79BF065DAC796FF8

FASTA933105,280
        10         20         30         40         50         60 
MAKISLKLDE LIDGEALRRE MTALTTATAG DGSGAAARAG VLQLLKARLA EGRKIAEAML 

        70         80         90        100        110        120 
KEDGGGNACA ERLSHLMDEL IRALYDFAAT HVYRVKNRSS AERMAVVAVG GYGRGTLAPG 

       130        140        150        160        170        180 
SDIDLLFLLP YKQTPWGEQT VEYMLYMLWD LGLKVGHATR NIDECLRLSR TDITIRTSIL 

       190        200        210        220        230        240 
EARFLWGERK LYDELMLRFD HEVVRTTGPE YVQAKLAERD ERHAKAGESR YLVEPNVKDG 

       250        260        270        280        290        300 
KGGLRDLQTL FWIGKYFYRV RTGEELVEKG VFTEAEYREF QKAEDFLWAV RCHMHFLTGK 

       310        320        330        340        350        360 
AEERLHFDIQ REIAERLGYT THPGLSAVER FMKHYFLVAK DVGDLTRIFC AALEEEQAKH 

       370        380        390        400        410        420 
VPGFNRIFLT FQRRKRKLAG TSDFIVDNHR INIADDQVFE RDPVNLLRLF WFADKHGLEF 

       430        440        450        460        470        480 
HPDALKLLTR SLGLVNKSLR RDEEANRLFL DILTSDRNAE LNLRRMNEAG LLGRLIPDFG 

       490        500        510        520        530        540 
KIVAMMQFSM YHHYTVDEHL IRCIGVLAEI ERGDGEKVHP LSHSLMPGLK KSREALYVAV 

       550        560        570        580        590        600 
LLHDIAKGRP EDHSEAGARI ARRICPHMGL SAADTETVAW LVENHLAMSM TAQTRDLNDR 

       610        620        630        640        650        660 
KTIEDFASIV QSVERLKLLL VLTVCDIRGV GPGVWNGWKG QLLRTLYYET ELLLTGGFSE 

       670        680        690        700        710        720 
VSRAQRTAAA RERLAEALAD WPDKDRKRYV GLHYENYLLT VDLPDQLRHA EFVREADAAG 

       730        740        750        760        770        780 
KKLATMVKTH QFEAVTEITV LAQDHPRLLS VIAGACVGAG GNIVDAQIFT TADGRALDTI 

       790        800        810        820        830        840 
LISREFDRDE DERRRAERVG RLIEDVLSGK SWLPEMIEKR TKPKRGAKVF KIPPRAEIRN 

       850        860        870        880        890        900 
TLSNRFSVIE VEGLDRPGLL SEITGTLSDL SLDIASAHIT TFGEKVIDTF YVTDLTGQKI 

       910        920        930 
DSPARIATIR NRLMATLEGI APERGGKAKA AAE 

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References

[1]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000012 Genomic DNA. Translation: BAB51794.1.
RefSeqNP_106008.1. NC_002678.2.

3D structure databases

ProteinModelPortalQ98C27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mll5321.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB51794; BAB51794; BAB51794.
GeneID1228669.
KEGGmlo:mll5321.
PATRIC22482678. VBIMesLot2464_4220.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-4157-MONOMER.

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_RHILO
AccessionPrimary (citable) accession number: Q98C27
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: October 1, 2001
Last modified: June 11, 2014
This is version 75 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