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P62223 (GLND_RHOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. 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:RPA0591
OrganismRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]
Taxonomic identifier258594 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

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 CAE26035.1 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_0000192762

Regions

Domain497 – 59296HD
Domain736 – 81883ACT 1
Domain849 – 92981ACT 2
Region1 – 379379Uridylyltransferase HAMAP-Rule MF_00277
Region380 – 735356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
P62223 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BC13BFA4845F8785

FASTA929104,542
        10         20         30         40         50         60 
MSPSRPAADE RFDSARVAAE IATLAEKHTG NDAAFRTALA MLMKAELAKA RTEAEAQLLR 

        70         80         90        100        110        120 
DRHGRRCAER LCYVQDAIIR LLFNAATEYL YNTPTPSSSE RMTVVATGGY GRGLMAPESD 

       130        140        150        160        170        180 
IDLLFILPYK QTAWGEQVAE VILYCLWDIG LKVGHATRSV DECIRQARAD MTIRTAILET 

       190        200        210        220        230        240 
RFLAGDEALY AELVERFDKE VVEGTAAEFV AAKLAEREER HRRSGQSRYL VEPNVKDGKG 

       250        260        270        280        290        300 
GLRDLHTLFW IAKYVYRVRE ASELSERGVF DPAEFRTFRR CEDFLWSVRC NIHFVTKRAE 

       310        320        330        340        350        360 
DRLSFDLQRE IGVRLGYTSH PGMQDVERFM KHYFLIAKEV GNLTAILCAK LEDQQAKAAP 

       370        380        390        400        410        420 
ALTRMMARLR PAAKRRRVPE SDDFVIDNNR INLAVPDVFK HDPVNLIRIF RLAQKNNLAF 

       430        440        450        460        470        480 
HPDAMRSVTR SLSLITPQLR DNPEANRLFV EILTSDNAEP VLRRMNETGV LGRFIRAFGR 

       490        500        510        520        530        540 
IVSMMQFNMY HSYTVDEHLI RCVGNLQEIE RGGNDEFALS SELIRKIRPD HRAVLYAAVL 

       550        560        570        580        590        600 
LHDIAKGQPE DHSTAGAKVA RRLCPRFGFS TADTELVAWL IEKHLVMSTV AQSRDLSDRK 

       610        620        630        640        650        660 
TIENFAAVVE TVEQMKMLTI LTTADIRGVG PGVWNGWKAQ LIRTLYYETE PVLTGGFSEV 

       670        680        690        700        710        720 
NRAERIRAAQ AEFRAAFTEW PEADLNAYVA RHYPAYWLKV DLQRKIRHAR FLRASEQAGH 

       730        740        750        760        770        780 
KLAINVGFDE ARAVTELTIL AVDHPWLLSV IAGACASAGA NIVDAQIYTT TDGRALDTIS 

       790        800        810        820        830        840 
ISREYDRDED EGRRATRIGE TIEEVLEGKL RLPEAVARRA SSGSKAKLRA FVVEPEVEIN 

       850        860        870        880        890        900 
NNWSDRYTVI EVSGLDRPGL LYQLTTAISK LNLNIASAHV ATFGERARDV FYVTDLLGAQ 

       910        920 
ITAPTRQAAI KRALVHLLAN GDAAEKPAA 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris."
Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S.
Nat. Biotechnol. 22:55-61(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-98 / CGA009.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX572594 Genomic DNA. Translation: CAE26035.1. Different initiation.
RefSeqNP_945944.1. NC_005296.1.

3D structure databases

ProteinModelPortalP62223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP62223. 1 interaction.
MINTMINT-6732844.
STRING258594.RPA0591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE26035; CAE26035; RPA0591.
GeneID2692917.
KEGGrpa:RPA0591.
PATRIC23285359. VBIRhoPal84835_0625.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OrthoDBEOG6CCH44.

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_RHOPA
AccessionPrimary (citable) accession number: P62223
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 69 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