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Q886P5

- GLND_PSESM

UniProt

Q886P5 - GLND_PSESM

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, PSPTO_1532
Organism
Pseudomonas syringae pv. tomato (strain DC3000)
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

BioCyciPSYR223283:GJIX-1559-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:PSPTO_1532
OrganismiPseudomonas syringae pv. tomato (strain DC3000)
Taxonomic identifieri223283 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002515: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 898898Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_0000192756Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi223283.PSPTO_1532.

Structurei

3D structure databases

ProteinModelPortaliQ886P5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini463 – 567105HD
Add
BLAST
Domaini705 – 78884ACT 1
Add
BLAST
Domaini815 – 89177ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 341341UridylyltransferaseUniRule annotation
Add
BLAST
Regioni342 – 704363Uridylyl-removingUniRule annotation
Add
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.
PhylomeDBiQ886P5.

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.

Q886P5-1 [UniParc]FASTAAdd to Basket

« Hide

MPQVDPDLFD RGQFQAELAL KASPIAAFKK AIRRARDVLD NRFRSGRDIR    50
RLIEDRAWFV DNILQQAWDQ FEWSEDADIA LLAVGGYGRG ELHPYSDIDL 100
LILLESDDHE VFREPIERFL TLLWDIGLEV GQSVRSVDEC AQEGRADLTV 150
ITNLMESRTI AGPEHLRQRM LEVTSTQHMW PSKEFFLAKH AEQKKRHHKY 200
NDTEYNLEPN VKGSPGGLRD IQTILWVARR QYGTLNLHAL AGEGFLLGSE 250
NALLASSQEF LWKVRYALHM LAGRSEDRLL FDYQVRIAGL LGYEDNDAKL 300
AIERFMQKYY RVVMSIAELS DLIIQHFEEV ILSDDDGTPQ PINSRFQLHD 350
GYIEATNPNV FRRTPFAMLE IFVLMAQHPE IKGVRADTIR LLREHRHLIN 400
DDFRNDIRNT SLFIELFKCE IGIHRNLRRM NRYGILGLYL PEFGHIVGQM 450
QHDLFHIYTV DAHTLNLIKH LRKLQYTEVS EKFPLASKIM ARLPKPELIY 500
LAGLYHDIGK GRGGDHSELG AVDAQAFGTR HHLPAWDNRL IVWLVSNHLV 550
MSTTAQRKDL SDPQVIHDFA QFVGDEVHLD YLYVLTVADI NATNPTLWNS 600
WRASLLRQLY TETKRALRRG LENPVDREEQ IRRTQTAALD ILVRSGTDPD 650
DVEQLWSALG DDYFLRHTAG DVAWHSDAIL QQPADGGPLV LIKETTQREF 700
EGGTQIFIYA PDQHDFFAVT VAAMDQLNLN IHDARIITSS SQFTLDTYIV 750
LDHEGGSIGN NPERIQDIRD GLTEALRNPD DYPTIIKRRV PRQLKHFAFA 800
PQVTIHNDAQ RPVTVLELLA PDRPGLLARI GKIFLEFDLS LQNAKIATLG 850
ERVEDVFFIT DANNQPLSDP QLCSQLQEAI VKQLSVNSEP GGDLRISI 898
Length:898
Mass (Da):102,738
Last modified:June 1, 2003 - v1
Checksum:i09151491E148C501
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016853 Genomic DNA. Translation: AAO55052.1.
RefSeqiNP_791357.1. NC_004578.1.

Genome annotation databases

EnsemblBacteriaiAAO55052; AAO55052; PSPTO_1532.
GeneIDi1183169.
KEGGipst:PSPTO_1532.
PATRICi19994312. VBIPseSyr93040_1556.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE016853 Genomic DNA. Translation: AAO55052.1 .
RefSeqi NP_791357.1. NC_004578.1.

3D structure databases

ProteinModelPortali Q886P5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 223283.PSPTO_1532.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAO55052 ; AAO55052 ; PSPTO_1532 .
GeneIDi 1183169.
KEGGi pst:PSPTO_1532.
PATRICi 19994312. VBIPseSyr93040_1556.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.
PhylomeDBi Q886P5.

Enzyme and pathway databases

BioCyci PSYR223283:GJIX-1559-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: DC3000.

Entry informationi

Entry nameiGLND_PSESM
AccessioniPrimary (citable) accession number: Q886P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 82 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

Similar proteinsi