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Q47F95

- GLND_DECAR

UniProt

Q47F95 - GLND_DECAR

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, Daro_1739
Organism
Dechloromonas aromatica (strain RCB)
Status
Reviewed - Annotation score: 4 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

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

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. metal ion binding Source: InterPro
  4. 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 enzyme
Short name:
UTase/UR
Alternative name(s):
Bifunctional [protein-PII] modification enzyme
Bifunctional nitrogen sensor protein
Including the following 2 domains:
[Protein-PII] uridylyltransferase (EC:2.7.7.59)
Short name:
PII uridylyltransferase
Short name:
UTase
[Protein-PII]-UMP uridylyl-removing enzyme (EC:3.1.4.-)
Short name:
UR
Gene namesi
Name:glnD
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 enzymeUniRule annotationPRO_0000231681Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi159087.Daro_1739.

Structurei

3D structure databases

ProteinModelPortaliQ47F95.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini437 – 53397HDAdd
BLAST
Domaini676 – 75580ACT 1Add
BLAST
Domaini784 – 85269ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 317317UridylyltransferaseUniRule annotationAdd
BLAST
Regioni318 – 675358Uridylyl-removingUniRule annotationAdd
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 By similarity.UniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiHHLLMSV.
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

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MSCDVAALRA EVKANQNQLR LNYEQSNDAV ALLRDRCQHV DTVLEKLWLS    50
LNFPASLALA AVGGYGRGEL YPASDIDLLI LLPQEASASL QEKLERLVGH 100
FWDIGLEIGH SVRTVQECLD EAANDITVQT ALLEARLLTG NTKLFATFQK 150
RLRGNLDPLH FFEAKRLEQQ ERYLRFNETP YSLEPNCKES PGGLRDIQVI 200
FWIAKAAGYG STWAELHQNG IITQEEMIQM EGCEAYLNHL RIRLHFMLGR 250
REDRLLFDYQ STLAANYGFV SNEAKRESEQ LMQVYYRNAK TVTVLNTILL 300
QNMGAALTPE SEQTPQQLDE SFQIVGNLLD IRDEQLYERN PLAILDSFLA 350
MQESHELFGM TARTLRALWR AREQITPEFR ANPENRAAFM KLLQGDRGIV 400
HEFRRMNQLG ILGRYLPNFG RIVGQMQHDL FHVYTVDQHI LQVMRNIRRF 450
TMSEFAHEYP LCSRIISELD RPWLLYVAAL FHDIAKGRGG DHSELGTVDT 500
REFCVNHGLS EEDTELVVWL VKNHLVMSQV AQKEDLSDPD VIANFIRLVG 550
DTRHLQALYL LTHADIRGTS PKVWNNWKGK LLADLYYQAI HHINQGEAPA 600
AHGVIAERQA EAMRLLRFFA LSATVHERLW KQLDTVYFLR HSAEEIAWHT 650
RSLHYRIYNN QPVVRARPNQ EGDGLQVMVY TQDQPDLFAR IVGFFARAGY 700
SIVDAKIHTT AHGYALDSFV VLDIEERDND REMVAYIEHE LEQRLLHQMP 750
RDVPSSGRLS RQVKHFPIKP EVSIRGDEKG THFILSLVAA DRPGLLYTVA 800
NTLTEHGAYL HTAKITTLGE RAEDVFLISG GDLRDTHNRI RLETELMERL 850
KV 852
Length:852
Mass (Da):97,701
Last modified:September 13, 2005 - v1
Checksum:iB60B7794DE1B3594
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
CP000089 Genomic DNA. Translation: AAZ46486.1 .
RefSeqi YP_284956.1. NC_007298.1.

3D structure databases

ProteinModelPortali Q47F95.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 159087.Daro_1739.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAZ46486 ; AAZ46486 ; Daro_1739 .
GeneIDi 3568481.
KEGGi dar:Daro_1739.
PATRICi 21602120. VBIDecAro89105_1724.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci DARO159087:GI5B-1793-MONOMER.

Family and domain databases

Gene3Di 1.10.3210.10. 1 hit.
HAMAPi MF_00277. PII_uridylyl_transf.
InterProi IPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF006288. PII_uridyltransf. 1 hit.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01693. UTase_glnD. 1 hit.
PROSITEi PS51671. ACT. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: June 11, 2014
This is version 66 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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