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Q89VX9 (GLND_BRADU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 71. 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:bll0916
OrganismBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110) [Reference proteome] [HAMAP]
Taxonomic identifier224911 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length929 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 caution

The sequence BAC46181.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 929929Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192721

Regions

Domain524 – 59774HD
Domain740 – 82283ACT 1
Domain850 – 92778ACT 2
Region1 – 383383Uridylyltransferase HAMAP-Rule MF_00277
Region384 – 739356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q89VX9 [UniParc].

Last modified July 5, 2004. Version 2.
Checksum: E4A270C497C26D5E

FASTA929105,033
        10         20         30         40         50         60 
MDSVTTEHKQ EVDDRFDTAR ITAAVDALAE KHQGREDAFR TAMAQLLKAE LIAARAAAQA 

        70         80         90        100        110        120 
ILLKDRHGRR CAERLCHVQD EIIRILYSAA TRHLYRSPIP SGAERMAVVA TGGYGRGLMA 

       130        140        150        160        170        180 
PESDIDLLFI LPYKQTAWGE QVAEAILYCL WDMGLKVGHA TRSVDESIRQ ARGDMTIRTA 

       190        200        210        220        230        240 
ILETRFLTGD QPLYDELVER FDKEVVQGTA SEFVTAKLAE REERHRRGGQ SRYLVEPNVK 

       250        260        270        280        290        300 
DGKGALRDLH TLFWIAKYVY RVRDTDELVE RGVFDAQEYR TFRRCADFLW SVRCNLHFYS 

       310        320        330        340        350        360 
GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLV AKEVGNLTAI LCAKLEDQQA 

       370        380        390        400        410        420 
KPAPVLSRMM ARLRPTPAKR RVPDSDDFIV DNNRINVAAP DVFKHDPVNL IRIFRLAQKH 

       430        440        450        460        470        480 
NLAFHPDAMR DVTRSLGLIN AQLRENPEAN RLFMEILTSD NAEIVLRRMN ETGVLGHFIR 

       490        500        510        520        530        540 
AFGKIVSMMQ FNMYHHYTVD EHLIRCVGFL QDIERGGIEE FAVASDLMRK IRPEHRSVIY 

       550        560        570        580        590        600 
IATLLHDVAK GRPEDHSIAG AKVARRLCPR LGFSPADTEL VAWLIEEHLT MSTVAQSRDL 

       610        620        630        640        650        660 
SDRKTIENFA AVVQSVEQMK LLTILTTADI RGVGPGVWNG WKAQLLRSLY YETEPVLTGG 

       670        680        690        700        710        720 
FSEVDRGKRL TAAYAEFRNA FAEWPADELD AYIARHYPAY WLKVELPRKI RHARFVRSSE 

       730        740        750        760        770        780 
QAGHKLAINV GFDEVRGVTE LTIFAADHPW LLSIIAGACA SAGANIVDAQ IYTTTDGRAL 

       790        800        810        820        830        840 
DTISISREYD RDEDEGRRAT RIGEMIEDVL EGKLRLPEVV ARRTVRSKAR PFVIEPEVTI 

       850        860        870        880        890        900 
NNQWSDRYTV IEVSGLDRPG LLYELTTAIS KLNLNIASAH VATFGERARD VFYVTDLLGA 

       910        920 
QINAPTRQSA IKSALTHVMA GDKAVQPAA 

« Hide

References

[1]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000040 Genomic DNA. Translation: BAC46181.1. Different initiation.
RefSeqNP_767556.1. NC_004463.1.

3D structure databases

ProteinModelPortalQ89VX9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224911.bll0916.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC46181; BAC46181; BAC46181.
GeneID1049859.
KEGGbja:bll0916.
PATRIC21185328. VBIBraJap65052_0935.

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycBJAP224911:GJEJ-925-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_BRADU
AccessionPrimary (citable) accession number: Q89VX9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 71 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