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Q9JUC9

- GLND_NEIMA

UniProt

Q9JUC9 - GLND_NEIMA

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, NMA1374
Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
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

BioCyciNMEN122587:GI3Q-1260-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:NMA1374
OrganismiNeisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Taxonomic identifieri122587 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000626: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_0000192747Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi122587.NMA1374.

Structurei

3D structure databases

ProteinModelPortaliQ9JUC9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini437 – 539103HD
Add
BLAST
Domaini673 – 75785ACT 1
Add
BLAST
Domaini785 – 85268ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 318318UridylyltransferaseUniRule annotation
Add
BLAST
Regioni319 – 672354Uridylyl-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.
OMAiLYCLWDM.
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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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.

Q9JUC9-1 [UniParc]FASTAAdd to Basket

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MPANLSSALE TFKQQRDAAE AHYLKANRVS VFFREYTAAV ETLLAALWAE    50
YFQNSALCLM AVGGFGRGEL YPCSDVDLAV VSPAPLSDGI QEQIARFVQT 100
LWDCKLMPSV KSGSVDELCE SVRNDITGDT AFLEARFLFG NRQTADKLAE 150
KMNAQRNVAA FVEAKLVEME HRHAKSQGSG AVLEPNIKSC PGGLRDIHTL 200
LWIAKAQGLA TDLPDLLKQR ILTRAEAGML SHGYRRLAHI RIHLHLNAKR 250
AEDRLLFDLQ PQVAESMGYE GLNLRRQSEE LMRVFYRAIK TVKQLSGILT 300
PMLRSRVSSA PMRVTLRIDD DYIQVNNQIA ARHTDIFFRR PEHIFKIVEI 350
MQQRNDITAL EPQTLRAWWG ATRKINRSFY QNSENRHRFA GFFRNGNGLT 400
QTLRFLNLYG VLGRYLPAWE KIVGLLQHDL FHIYPVDDHI LTVVRNVRRL 450
ALDMHSHELP YASALMQSFE KQDILYLAAF FHDIAKGRGG DHAIQGIADA 500
RQFAADHFLT GEESDLLAWL VENHLLMSAV AQKEDIQDPD VLDAFCKRVQ 550
THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RYLTGNGGNP 600
HTLFGRRRQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA 650
NLVHDFETPI VRSRILFKSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL 700
AARAFITEHD YILDTFIVQI PSQHAPEDYP DIQSALEAEL NSFIHGHTVA 750
ETQSHSRRIS RRSRYMPIAP SITITPEEDY PDWYSVEITA VNRPFLLADM 800
AEVFFAHNVS LRYAKISTLD ERAEDSFTVF SLDLKNPKIQ SSLKQTLLEQ 850
LS 852
Length:852
Mass (Da):97,058
Last modified:October 1, 2000 - v1
Checksum:i1FA6E76877BEF9F9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL157959 Genomic DNA. Translation: CAM08547.1.
PIRiH81906.
RefSeqiYP_002342728.1. NC_003116.1.

Genome annotation databases

EnsemblBacteriaiCAM08547; CAM08547; NMA1374.
GeneIDi907781.
KEGGinma:NMA1374.
PATRICi20363789. VBINeiMen132687_1600.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL157959 Genomic DNA. Translation: CAM08547.1 .
PIRi H81906.
RefSeqi YP_002342728.1. NC_003116.1.

3D structure databases

ProteinModelPortali Q9JUC9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 122587.NMA1374.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAM08547 ; CAM08547 ; NMA1374 .
GeneIDi 907781.
KEGGi nma:NMA1374.
PATRICi 20363789. VBINeiMen132687_1600.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NMEN122587:GI3Q-1260-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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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: Z2491.

Entry informationi

Entry nameiGLND_NEIMA
AccessioniPrimary (citable) accession number: Q9JUC9
Secondary accession number(s): A1IRZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 86 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