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Q6LN22 (GLND_PHOPR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. 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:PBPRA2970
OrganismPhotobacterium profundum (Photobacterium sp. (strain SS9)) [Complete proteome] [HAMAP]
Taxonomic identifier74109 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length874 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 assimilation 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 – 874874Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192750

Regions

Domain455 – 588134HD
Domain696 – 77984ACT 1
Domain802 – 87473ACT 2
Region1 – 336336Uridylyltransferase HAMAP-Rule MF_00277
Region337 – 695359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q6LN22 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: BD18CA770614C067

FASTA874100,797
        10         20         30         40         50         60 
MIDTSTITNP QTLPVEAITQ ENLRNTLEQF AEQQKQQFIQ HRPVTDLVLS RSTFIDKLLI 

        70         80         90        100        110        120 
RLWEHYEVNQ YPDIALVAVG GYGRGELHPL SDVDILILSA QPLSDETGRI VSKFLTFLWD 

       130        140        150        160        170        180 
LRLEVGHSVR TIDDCIEIGN DDLTVATNLT EARILCGSED VFQCLQERIN AGNFWPSEDF 

       190        200        210        220        230        240 
YRAKLEEQKT RHARYHDTTY NLEPDIKSSP GGLRDIHTLS WVARRHFGAT SLLEMSRFGF 

       250        260        270        280        290        300 
LTDAEYRELV ECQDSLWRIR FALHIELRRY DNRLTFSHQP SVAENLGYTG EGNRGVEMMM 

       310        320        330        340        350        360 
KEFYRTLRRV LELNKMLLQL FDQAILDNGK TVETIQLSDD FQIRGHLIEA TKPALFQARP 

       370        380        390        400        410        420 
ETILDMFLHI AQNGDIEGIA APTLRQLRTA RQRLNVFLVD IPEAREKFME LVRQPNTLQK 

       430        440        450        460        470        480 
AFRLMHRHGV LSAYLPQWSQ IVGQMQFDLF HVYTVDEHSV RLIKNLNKFN DPENRERHPI 

       490        500        510        520        530        540 
CCEVYPRIIK KELLTIAAIF HDIAKGRGGD HSELGAIEAR KFCIQHGLSR PETNLIAWLV 

       550        560        570        580        590        600 
QKHLLMSVTA QRRDIYDPEV VAEFAKEVRD EERLDYLICL TVADICATNQ ELWNSWKRTL 

       610        620        630        640        650        660 
LAELYYSTQK ALRRGLENTP DVRDRIRHNQ QLSSAILRGK GFAPREIEVL WKRFKADYFL 

       670        680        690        700        710        720 
RHTHKQLAWH AEALLTHDHD KPLILLSKKA TRGGTEVFVY NKDKAKLFAI VVSELDKKNL 

       730        740        750        760        770        780 
SVHDAQIMNS KDGYTLDTFM VLDPSGKTIP ENRHNTIRRA LVNALTKMKS ERKNKRAPRK 

       790        800        810        820        830        840 
LMHFNVKTQV DFLPTKTGKK TTMELIALDT PGLLARIGAV FAKQKVSLQA AKITTIGERA 

       850        860        870 
EDFFILVNEH GSPLTEEHQQ ALKEALIIKL TPQD 

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References

[1]"Life at depth: Photobacterium profundum genome sequence and expression analysis."
Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., Bartlett D.H., Valle G.
Science 307:1459-1461(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SS9.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR378672 Genomic DNA. Translation: CAG21304.1.
RefSeqYP_131106.1. NC_006370.1.

3D structure databases

ProteinModelPortalQ6LN22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING298386.PBPRA2970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAG21304; CAG21304; PBPRA2970.
GeneID3123062.
KEGGppr:PBPRA2970.
PATRIC22936978. VBIPhoPro109272_3134.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
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. 1 hit.
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_PHOPR
AccessionPrimary (citable) accession number: Q6LN22
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: July 5, 2004
Last modified: June 11, 2014
This is version 70 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