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A1KU16

- GLND_NEIMF

UniProt

A1KU16 - GLND_NEIMF

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, NMC1104
Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
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

BioCyciNMEN272831:GJDX-1063-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:NMC1104
OrganismiNeisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Taxonomic identifieri272831 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000002286: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000022347Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272831.NMC1104.

Structurei

3D structure databases

ProteinModelPortaliA1KU16.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 318318UridylyltransferaseUniRule annotationAdd
BLAST
Regioni319 – 672354Uridylyl-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.
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.

A1KU16-1 [UniParc]FASTAAdd to Basket

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MPANLSSALE TFKQQRDAAE AHYLKTNRVS VFFREYTAAV ETLLAALWVE    50
HFQNSALCLM AVGGFGRGEL YPCSDVDLAV VSPAPLSDGI QEQIARFVQT 100
LWDCKLMPSV KSGGIDELCE SVRNDITGDT AFLEARFLFG NRQTADELAE 150
KMNAQRNVAA FIEAKLVEME HRHAKSQGSG AVLEPNIKSC PGGLRDIHTL 200
LWIAKAQGLA TNLPALVKQG ILTRTEAGML SHGYRRLAHI RIHLHLNAKR 250
AEDRLLFDLQ PQVAESMGYQ GLNLRRQSEE LMRVFYRAIK TVKQLSGILT 300
PMLQSRVSST PLRVTLRIDD DYIQVNNQIA ARHTDIFFRR PEHIFKIVEI 350
MQQRNDITAL EPQTLRAWWG ATRKINRSFY QNSENRHRFA GFFRNGNGLT 400
QTLRFLNLYG VLGRYLPAWE KIVGLLQHDL FHIYPVDDHI LTVVRNVRRL 450
ALDMHSHELP YASALMQSFE RQDILYLAAF FHDIAKGRGG DHAIQGIADA 500
RQFAADHFLT EEESDLLAWL VENHLLMSTV AQKEDIQDPS VLDAFCKRVQ 550
THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RYLAGNGGNP 600
HALFGRRQQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA 650
NLVHDFETPI VRSRILPQSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL 700
AARAFITEHD YILDTFIVQI PSQHAPEDYP DIQSALEAEL NSFIHGHTVA 750
EISSHSRRIS RRSRYMPIAP SITITPEEDY PDWYSVEITA VNRPFLLADM 800
AEIFFAHNVS LRYAKISTLD ERAEDSFTVF SPDLKNPKIQ SSLKQALLEQ 850
LA 852
Length:852
Mass (Da):96,831
Last modified:February 6, 2007 - v1
Checksum:iD9A8CF7651CA2409
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM421808 Genomic DNA. Translation: CAM10357.1.
RefSeqiYP_975145.1. NC_008767.1.

Genome annotation databases

EnsemblBacteriaiCAM10357; CAM10357; NMC1104.
GeneIDi4676490.
KEGGinmc:NMC1104.
PATRICi20352183. VBINeiMen17609_1341.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM421808 Genomic DNA. Translation: CAM10357.1 .
RefSeqi YP_975145.1. NC_008767.1.

3D structure databases

ProteinModelPortali A1KU16.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272831.NMC1104.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAM10357 ; CAM10357 ; NMC1104 .
GeneIDi 4676490.
KEGGi nmc:NMC1104.
PATRICi 20352183. VBINeiMen17609_1341.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NMEN272831:GJDX-1063-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: ATCC 700532 / DSM 15464 / FAM18.

Entry informationi

Entry nameiGLND_NEIMF
AccessioniPrimary (citable) accession number: A1KU16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: June 11, 2014
This is version 57 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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