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Q1LNG0 (GLND_RALME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Rmet_1433
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length857 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 – 857857Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000078810

Regions

Domain442 – 544103HD
Domain680 – 76081ACT 1
Domain788 – 85770ACT 2
Region1 – 322322Uridylyltransferase HAMAP-Rule MF_00277
Region323 – 679357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q1LNG0 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: 0BFF1E5B9F7498A8

FASTA85797,774
        10         20         30         40         50         60 
MDTTPELLLC QRIRDKLKAD KQVLFAEFDA NNQVNPLVTK LRRAVDVALT EAWTGLELPG 

        70         80         90        100        110        120 
DVALVAVGGY GRGELFPHSD VDVLLLLPGE PDAKMAAKLE RFIGLCWDLG LEIGSSVRTV 

       130        140        150        160        170        180 
DDCIRESAAD ITIRTSLLEA RLLIGNKALF KSLQTRYQAD MDAADFFQAK LLEMRQRHAK 

       190        200        210        220        230        240 
YQDTPYALEP NCKESPGGLR DLQVILWMTE AARLGDSWKQ LFERGLLTER EAQELTRNER 

       250        260        270        280        290        300 
LLRTIRARLH LLAGRRQDVL VFDLQTALAE AFGYRQTTNK RASEQLMRRY YWAAKAVTQL 

       310        320        330        340        350        360 
NSVLLLNIEA MLFPSESMVT REINDRFVER QGMLEITSDD LYERNPHAIL ETFLLYERTP 

       370        380        390        400        410        420 
GVKGLSPRTL RGLYNARTVM DASWRNDPVN RRLFLAIVQE PQGITHALRL MNQTSVLGRY 

       430        440        450        460        470        480 
LINFRRIVGQ MQHDLFHVYT VDQHILMVVR NMRRFAIVEH THEFPFCSQL MAGFDRPWVL 

       490        500        510        520        530        540 
WVAALFHDIA KGRGGDHSKL GTVDARRFCK QHGISREDTD LIAWLVEHHL TMSHVAQKQD 

       550        560        570        580        590        600 
LTDPDVVKAF AQVVGNGRYL TALYLLTVAD IRGTSPKVWN AWKGKLLEDL YRITLRVLGG 

       610        620        630        640        650        660 
ARLDTHSLWA QKRDDTIAQL RLKAFDPELA KPLWDKLDMS FFMRQDARDI AWLTRSLFNK 

       670        680        690        700        710        720 
VNSPNPVVKA RISPAGEGLQ VAVYVKDQPD LFARICGYFE RKAFSIQDAK IETTRDGYAL 

       730        740        750        760        770        780 
DTFQITDPGL AGDYRDILTL VEHELGERVR LECPLPDPTQ GRLSRQSRSF PIKPRVDLRP 

       790        800        810        820        830        840 
DERGQYYLLS VSANDRTGLL YAIARVLAKH RVSVHSARIN TLGERVEDVF LVDGSRLAAD 

       850 
NRLQIQLEQD LLDALAI 

« Hide

References

[1]"Complete sequence of the chromosome of Ralstonia metallidurans CH34."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000352 Genomic DNA. Translation: ABF08316.1.
RefSeqYP_583585.1. NC_007973.1.

3D structure databases

ProteinModelPortalQ1LNG0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266264.Rmet_1433.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF08316; ABF08316; Rmet_1433.
GeneID4038236.
KEGGrme:Rmet_1433.
PATRIC20287480. VBIRalMet4734_1842.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK03059.

Enzyme and pathway databases

BioCycCMET266264:GJ5G-1494-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_RALME
AccessionPrimary (citable) accession number: Q1LNG0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 30, 2006
Last modified: February 19, 2014
This is version 60 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