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Q47F95 (GLND_DECAR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. 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:Daro_1739
OrganismDechloromonas aromatica (strain RCB) [Complete proteome] [HAMAP]
Taxonomic identifier159087 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas

Protein attributes

Sequence length852 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 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231681

Regions

Domain437 – 53397HD
Domain676 – 75580ACT 1
Domain784 – 85269ACT 2
Region1 – 317317Uridylyltransferase HAMAP-Rule MF_00277
Region318 – 675358Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q47F95 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: B60B7794DE1B3594

FASTA85297,701
        10         20         30         40         50         60 
MSCDVAALRA EVKANQNQLR LNYEQSNDAV ALLRDRCQHV DTVLEKLWLS LNFPASLALA 

        70         80         90        100        110        120 
AVGGYGRGEL YPASDIDLLI LLPQEASASL QEKLERLVGH FWDIGLEIGH SVRTVQECLD 

       130        140        150        160        170        180 
EAANDITVQT ALLEARLLTG NTKLFATFQK RLRGNLDPLH FFEAKRLEQQ ERYLRFNETP 

       190        200        210        220        230        240 
YSLEPNCKES PGGLRDIQVI FWIAKAAGYG STWAELHQNG IITQEEMIQM EGCEAYLNHL 

       250        260        270        280        290        300 
RIRLHFMLGR REDRLLFDYQ STLAANYGFV SNEAKRESEQ LMQVYYRNAK TVTVLNTILL 

       310        320        330        340        350        360 
QNMGAALTPE SEQTPQQLDE SFQIVGNLLD IRDEQLYERN PLAILDSFLA MQESHELFGM 

       370        380        390        400        410        420 
TARTLRALWR AREQITPEFR ANPENRAAFM KLLQGDRGIV HEFRRMNQLG ILGRYLPNFG 

       430        440        450        460        470        480 
RIVGQMQHDL FHVYTVDQHI LQVMRNIRRF TMSEFAHEYP LCSRIISELD RPWLLYVAAL 

       490        500        510        520        530        540 
FHDIAKGRGG DHSELGTVDT REFCVNHGLS EEDTELVVWL VKNHLVMSQV AQKEDLSDPD 

       550        560        570        580        590        600 
VIANFIRLVG DTRHLQALYL LTHADIRGTS PKVWNNWKGK LLADLYYQAI HHINQGEAPA 

       610        620        630        640        650        660 
AHGVIAERQA EAMRLLRFFA LSATVHERLW KQLDTVYFLR HSAEEIAWHT RSLHYRIYNN 

       670        680        690        700        710        720 
QPVVRARPNQ EGDGLQVMVY TQDQPDLFAR IVGFFARAGY SIVDAKIHTT AHGYALDSFV 

       730        740        750        760        770        780 
VLDIEERDND REMVAYIEHE LEQRLLHQMP RDVPSSGRLS RQVKHFPIKP EVSIRGDEKG 

       790        800        810        820        830        840 
THFILSLVAA DRPGLLYTVA NTLTEHGAYL HTAKITTLGE RAEDVFLISG GDLRDTHNRI 

       850 
RLETELMERL KV 

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References

[1]"Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB: indications of a surprisingly complex life-style and cryptic anaerobic pathways for aromatic degradation."
Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G., Lapidus A.
BMC Genomics 10:351-351(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RCB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000089 Genomic DNA. Translation: AAZ46486.1.
RefSeqYP_284956.1. NC_007298.1.

3D structure databases

ProteinModelPortalQ47F95.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING159087.Daro_1739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ46486; AAZ46486; Daro_1739.
GeneID3568481.
KEGGdar:Daro_1739.
PATRIC21602120. VBIDecAro89105_1724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycDARO159087:GI5B-1793-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. 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_DECAR
AccessionPrimary (citable) accession number: Q47F95
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2005
Last modified: June 11, 2014
This is version 66 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