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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Dechloromonas aromatica (strain RCB)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity.UniRule annotation

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. nitrogen compound metabolic process Source: InterPro
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciDARO159087:GI5B-1793-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
Short name:
UTase/URUniRule annotation
Alternative name(s):
Bifunctional [protein-PII] modification enzymeUniRule annotation
Bifunctional nitrogen sensor proteinUniRule annotation
Including the following 2 domains:
[Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
Short name:
PII uridylyltransferaseUniRule annotation
Short name:
UTaseUniRule annotation
[Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
Short name:
URUniRule annotation
Gene namesi
Name:glnDUniRule annotation
Ordered Locus Names:Daro_1739
OrganismiDechloromonas aromatica (strain RCB)
Taxonomic identifieri159087 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeDechloromonas
ProteomesiUP000000550: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231681Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi159087.Daro_1739.

Structurei

3D structure databases

ProteinModelPortaliQ47F95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini437 – 53397HDUniRule annotationAdd
BLAST
Domaini676 – 75580ACT 1UniRule annotationAdd
BLAST
Domaini784 – 85269ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 317317UridylyltransferaseAdd
BLAST
Regioni318 – 675358Uridylyl-removingAdd
BLAST

Domaini

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.UniRule annotation

Sequence similaritiesi

Belongs to the GlnD family.UniRule annotation
Contains 2 ACT domains.UniRule annotation
Contains 1 HD domain.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiCFATVTG.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q47F95-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSCDVAALRA EVKANQNQLR LNYEQSNDAV ALLRDRCQHV DTVLEKLWLS
60 70 80 90 100
LNFPASLALA AVGGYGRGEL YPASDIDLLI LLPQEASASL QEKLERLVGH
110 120 130 140 150
FWDIGLEIGH SVRTVQECLD EAANDITVQT ALLEARLLTG NTKLFATFQK
160 170 180 190 200
RLRGNLDPLH FFEAKRLEQQ ERYLRFNETP YSLEPNCKES PGGLRDIQVI
210 220 230 240 250
FWIAKAAGYG STWAELHQNG IITQEEMIQM EGCEAYLNHL RIRLHFMLGR
260 270 280 290 300
REDRLLFDYQ STLAANYGFV SNEAKRESEQ LMQVYYRNAK TVTVLNTILL
310 320 330 340 350
QNMGAALTPE SEQTPQQLDE SFQIVGNLLD IRDEQLYERN PLAILDSFLA
360 370 380 390 400
MQESHELFGM TARTLRALWR AREQITPEFR ANPENRAAFM KLLQGDRGIV
410 420 430 440 450
HEFRRMNQLG ILGRYLPNFG RIVGQMQHDL FHVYTVDQHI LQVMRNIRRF
460 470 480 490 500
TMSEFAHEYP LCSRIISELD RPWLLYVAAL FHDIAKGRGG DHSELGTVDT
510 520 530 540 550
REFCVNHGLS EEDTELVVWL VKNHLVMSQV AQKEDLSDPD VIANFIRLVG
560 570 580 590 600
DTRHLQALYL LTHADIRGTS PKVWNNWKGK LLADLYYQAI HHINQGEAPA
610 620 630 640 650
AHGVIAERQA EAMRLLRFFA LSATVHERLW KQLDTVYFLR HSAEEIAWHT
660 670 680 690 700
RSLHYRIYNN QPVVRARPNQ EGDGLQVMVY TQDQPDLFAR IVGFFARAGY
710 720 730 740 750
SIVDAKIHTT AHGYALDSFV VLDIEERDND REMVAYIEHE LEQRLLHQMP
760 770 780 790 800
RDVPSSGRLS RQVKHFPIKP EVSIRGDEKG THFILSLVAA DRPGLLYTVA
810 820 830 840 850
NTLTEHGAYL HTAKITTLGE RAEDVFLISG GDLRDTHNRI RLETELMERL

KV
Length:852
Mass (Da):97,701
Last modified:September 13, 2005 - v1
Checksum:iB60B7794DE1B3594
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA. Translation: AAZ46486.1.
RefSeqiYP_284956.1. NC_007298.1.

Genome annotation databases

EnsemblBacteriaiAAZ46486; AAZ46486; Daro_1739.
GeneIDi3568481.
KEGGidar:Daro_1739.
PATRICi21602120. VBIDecAro89105_1724.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000089 Genomic DNA. Translation: AAZ46486.1.
RefSeqiYP_284956.1. NC_007298.1.

3D structure databases

ProteinModelPortaliQ47F95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi159087.Daro_1739.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ46486; AAZ46486; Daro_1739.
GeneIDi3568481.
KEGGidar:Daro_1739.
PATRICi21602120. VBIDecAro89105_1724.

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiCFATVTG.
OrthoDBiEOG6CCH44.

Enzyme and pathway databases

BioCyciDARO159087:GI5B-1793-MONOMER.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiGLND_DECAR
AccessioniPrimary (citable) accession number: Q47F95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: September 13, 2005
Last modified: January 7, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.