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Q2GAJ4 (GLND_NOVAD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:Saro_0682
OrganismNovosphingobium aromaticivorans (strain DSM 12444) [Complete proteome] [HAMAP]
Taxonomic identifier279238 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeNovosphingobium

Protein attributes

Sequence length912 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 – 912912Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000078807

Regions

Domain486 – 591106HD
Domain723 – 80280ACT 1
Domain834 – 91279ACT 2
Region1 – 369369Uridylyltransferase HAMAP-Rule MF_00277
Region370 – 722353Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q2GAJ4 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: E81AD196FA1A216A

FASTA912101,972
        10         20         30         40         50         60 
MLPRIANQRA IVDRRALADA VSAAFAEQGD RSRPAVVELL RGALDSGRAE LARRLEARPS 

        70         80         90        100        110        120 
AGTECAHGQA FLVDQLVRVI HDHVVGKVYR ASNRSTGERI AIIAVGGYGR GEMAPHSDVD 

       130        140        150        160        170        180 
IAFVTPIKPT SWCEQVIEAI LYFLWDLGLK VGHSSRSLDE VVRMAKSDLT IRTALLEGRY 

       190        200        210        220        230        240 
VWGDRDLFDA ASARFWNEVV NGTEKQFVAE KLQERNERHK RLGDSRYVVE PNVKEGKGGL 

       250        260        270        280        290        300 
RDLHTLYWIG KYIHKVRDAS ELVDVGLLTA EEYRAFRRAE NFFWAVRCHL HAITRRAEDR 

       310        320        330        340        350        360 
LTFDLQREVA MRMNFADRPG KSAVERFMQY FFLQAKQVGS LTGVFLAQLD GQFARQKRSF 

       370        380        390        400        410        420 
FASLRSRRKK VGPFFIEGGK LGVPAEDTFQ QDPVRLVELF AVAASEKVEI HPEAMRLARR 

       430        440        450        460        470        480 
DAGLIDAAVR KDQRANALFL DVLTSRNDPE TVLRWMNEAG VFGRFVPDFG RVVAQMQFDM 

       490        500        510        520        530        540 
YHHYTVDEHT IRAIGLLASI EKGEAKADHP LASEVVGKVA SRRVLYVATL LHDIAKGRRG 

       550        560        570        580        590        600 
DHSVLGAEVA MKLCPRLGLS AAETELVAWL VRWHLLMSAT AFKRDLADYK TIADFVNTVQ 

       610        620        630        640        650        660 
SQERLRLLLL LTIVDIRAVG PGVWNSWKRQ LLGDLFVSAE EVLRLGHKQH GRAERIIAKK 

       670        680        690        700        710        720 
KAVGAILKER DNLIGTVGRQ LGDAYWIAEP EDIIALNLQQ MDQALGELLS VEAHWYPARG 

       730        740        750        760        770        780 
ATLVTVLAAD HPGLFYRIAG GIHLAGGNII DARIHTARNG TAVDNFLVQD PLGRPLNEAS 

       790        800        810        820        830        840 
QIERLKNAIA DALANRVKLV PQLAARPLAR PRADAFDVRP IVIFDNKASN RFTVIEVGAR 

       850        860        870        880        890        900 
DRPALLNRLA RALFEARLIV HSAHIATYGE RAVDTFYVTD VLGEKVDSEA RMKAVEKRLL 

       910 
EAAEDRKVKD AA 

« Hide

References

[1]"Complete sequence of Novosphingobium aromaticivorans DSM 12444."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N. expand/collapse author list , Fredrickson J., Balkwill D., Romine M.F., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 12444.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000248 Genomic DNA. Translation: ABD25129.1.
RefSeqYP_495963.1. NC_007794.1.

3D structure databases

ProteinModelPortalQ2GAJ4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279238.Saro_0682.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD25129; ABD25129; Saro_0682.
GeneID3918107.
KEGGnar:Saro_0682.
PATRIC22783982. VBINovAro50627_0701.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05092.

Enzyme and pathway databases

BioCycNARO279238:GHBU-690-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]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
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_NOVAD
AccessionPrimary (citable) accession number: Q2GAJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 21, 2006
Last modified: February 19, 2014
This is version 65 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