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Q1LNG0

- GLND_RALME

UniProt

Q1LNG0 - GLND_RALME

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Status
Reviewed - 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

BioCyciCMET266264:GJ5G-1494-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:Rmet_1433
OrganismiRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Taxonomic identifieri266264 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
ProteomesiUP000002429: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 857857Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000078810Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi266264.Rmet_1433.

Structurei

3D structure databases

ProteinModelPortaliQ1LNG0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini442 – 544103HDUniRule annotationAdd
BLAST
Domaini680 – 76081ACT 1UniRule annotationAdd
BLAST
Domaini788 – 85770ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 322322UridylyltransferaseAdd
BLAST
Regioni323 – 679357Uridylyl-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.
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.

Q1LNG0-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MDTTPELLLC QRIRDKLKAD KQVLFAEFDA NNQVNPLVTK LRRAVDVALT
60 70 80 90 100
EAWTGLELPG DVALVAVGGY GRGELFPHSD VDVLLLLPGE PDAKMAAKLE
110 120 130 140 150
RFIGLCWDLG LEIGSSVRTV DDCIRESAAD ITIRTSLLEA RLLIGNKALF
160 170 180 190 200
KSLQTRYQAD MDAADFFQAK LLEMRQRHAK YQDTPYALEP NCKESPGGLR
210 220 230 240 250
DLQVILWMTE AARLGDSWKQ LFERGLLTER EAQELTRNER LLRTIRARLH
260 270 280 290 300
LLAGRRQDVL VFDLQTALAE AFGYRQTTNK RASEQLMRRY YWAAKAVTQL
310 320 330 340 350
NSVLLLNIEA MLFPSESMVT REINDRFVER QGMLEITSDD LYERNPHAIL
360 370 380 390 400
ETFLLYERTP GVKGLSPRTL RGLYNARTVM DASWRNDPVN RRLFLAIVQE
410 420 430 440 450
PQGITHALRL MNQTSVLGRY LINFRRIVGQ MQHDLFHVYT VDQHILMVVR
460 470 480 490 500
NMRRFAIVEH THEFPFCSQL MAGFDRPWVL WVAALFHDIA KGRGGDHSKL
510 520 530 540 550
GTVDARRFCK QHGISREDTD LIAWLVEHHL TMSHVAQKQD LTDPDVVKAF
560 570 580 590 600
AQVVGNGRYL TALYLLTVAD IRGTSPKVWN AWKGKLLEDL YRITLRVLGG
610 620 630 640 650
ARLDTHSLWA QKRDDTIAQL RLKAFDPELA KPLWDKLDMS FFMRQDARDI
660 670 680 690 700
AWLTRSLFNK VNSPNPVVKA RISPAGEGLQ VAVYVKDQPD LFARICGYFE
710 720 730 740 750
RKAFSIQDAK IETTRDGYAL DTFQITDPGL AGDYRDILTL VEHELGERVR
760 770 780 790 800
LECPLPDPTQ GRLSRQSRSF PIKPRVDLRP DERGQYYLLS VSANDRTGLL
810 820 830 840 850
YAIARVLAKH RVSVHSARIN TLGERVEDVF LVDGSRLAAD NRLQIQLEQD

LLDALAI
Length:857
Mass (Da):97,774
Last modified:May 30, 2006 - v1
Checksum:i0BFF1E5B9F7498A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000352 Genomic DNA. Translation: ABF08316.1.
RefSeqiYP_583585.1. NC_007973.1.

Genome annotation databases

EnsemblBacteriaiABF08316; ABF08316; Rmet_1433.
GeneIDi4038236.
KEGGirme:Rmet_1433.
PATRICi20287480. VBIRalMet4734_1842.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000352 Genomic DNA. Translation: ABF08316.1 .
RefSeqi YP_583585.1. NC_007973.1.

3D structure databases

ProteinModelPortali Q1LNG0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 266264.Rmet_1433.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABF08316 ; ABF08316 ; Rmet_1433 .
GeneIDi 4038236.
KEGGi rme:Rmet_1433.
PATRICi 20287480. VBIRalMet4734_1842.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci CMET266264:GJ5G-1494-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CH34 / ATCC 43123 / DSM 2839.

Entry informationi

Entry nameiGLND_RALME
AccessioniPrimary (citable) accession number: Q1LNG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 30, 2006
Last modified: November 26, 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3