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Q8XZJ3

- GLND_RALSO

UniProt

Q8XZJ3 - GLND_RALSO

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, RSc1402, RS05290
Organism
Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
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

BioCyciRSOL267608:GCVU-1424-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:RSc1402
ORF Names:RS05290
OrganismiRalstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum)
Taxonomic identifieri267608 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeRalstonia
ProteomesiUP000001436: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 861861Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_0000192757Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi267608.RSc1402.

Structurei

3D structure databases

ProteinModelPortaliQ8XZJ3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini442 – 558117HDAdd
BLAST
Domaini680 – 76384ACT 1Add
BLAST
Domaini792 – 86170ACT 2Add
BLAST

Region

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

Q8XZJ3-1 [UniParc]FASTAAdd to Basket

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MHTAAAATPA TSPRDILKAE RAHLFAQFEQ HANVNLLVTK LARAVDQALI    50
LLWQDEGMPD TCALVAVGGY GRGELFPHSD VDILLLLPQT ADKALETRLE 100
AFIGHCWDMG LDIGSSVRTV DECISEATQD VTVCTSLLEA RLLTGDEGLY 150
RTFETHYQGH LDAADFYQSK MLEMRQRHAK YQDTPYSLEP NCKESPGGLR 200
DLQVILWMTR AAGFGSSWNE LLVNQLLTRR EAKELAANER LLKTIRARLH 250
LLAGRRQDVL VFDLQTQLGE AFGYRPNAAK RTSEQLMRRY YWAAKAVTQL 300
NTVVLQNIEA RLFPTELGIT RTINGRFVER QGMLEIADPE LYQREPAAIL 350
ETFLVYEQTR GVKGLAANTL RALYNARTQM DARWRRDPAN RATFLSILQQ 400
PQGITHALRL MNQTSVLGRY LVNFRRIVGQ MQHDLFHVYT VDQHILMVVR 450
NVRRFAIVEH AHEFPFCSQL MANFDKPWVL TVAALFHDIA KGRGGDHSVL 500
GMADARRFCK QHGIASEDAD LIVWLVEHHL TMSQVAQKQD LGDPEVIRHF 550
ADQVGSERYL SALYLLTVAD IRGTSPKVWN AWKAKLLEDL YRITLRVLGG 600
ATTDPHAVLE GRKEEARVLL RLAAMDPHAH EALWAQLDVG VFLRHDARDI 650
AWFTRHFYNR VDTTLPIVRA RISPVGEGLQ VAVYSPDRPD LFARICGYFE 700
RKGLTILDAK IHTTKHGYAL DTFQVADPGS GLVEPGHYRD IITLVEHELA 750
ELIARETVLA EPPRGRISRQ SRSFPIKPRV DLRPDERGQY YLLSLSATDR 800
TGLLYAIARV LARHRVSVHT ARINTLGERV EDVFLLDGRR LTQDNKLQLA 850
LESELLEALA I 861
Length:861
Mass (Da):97,493
Last modified:March 1, 2002 - v1
Checksum:i3C4F9172C180F7C0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL646052 Genomic DNA. Translation: CAD15104.1.
RefSeqiNP_519523.1. NC_003295.1.
WP_011001351.1. NC_003295.1.

Genome annotation databases

EnsemblBacteriaiCAD15104; CAD15104; RSc1402.
GeneIDi1220226.
KEGGirso:RSc1402.
PATRICi20261435. VBIRalSol70888_1432.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL646052 Genomic DNA. Translation: CAD15104.1 .
RefSeqi NP_519523.1. NC_003295.1.
WP_011001351.1. NC_003295.1.

3D structure databases

ProteinModelPortali Q8XZJ3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 267608.RSc1402.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAD15104 ; CAD15104 ; RSc1402 .
GeneIDi 1220226.
KEGGi rso:RSc1402.
PATRICi 20261435. VBIRalSol70888_1432.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci RSOL267608:GCVU-1424-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: GMI1000.

Entry informationi

Entry nameiGLND_RALSO
AccessioniPrimary (citable) accession number: Q8XZJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: March 1, 2002
Last modified: September 3, 2014
This is version 80 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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