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Q2L165

- GLND_BORA1

UniProt

Q2L165 - GLND_BORA1

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Bordetella avium (strain 197N)
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

BioCyciBAVI360910:GCKI-1759-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:BAV1732
OrganismiBordetella avium (strain 197N)
Taxonomic identifieri360910 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001977: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 858858Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000022326Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi360910.BAV1732.

Structurei

3D structure databases

ProteinModelPortaliQ2L165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini438 – 550113HDUniRule annotationAdd
BLAST
Domaini675 – 75682ACT 1UniRule annotationAdd
BLAST
Domaini789 – 85870ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 318318UridylyltransferaseAdd
BLAST
Regioni319 – 674356Uridylyl-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.
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.
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.

Q2L165-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPTDLHPIK ERMQAARAAA IADFRQHLRP DPLLSELRRI VDQALRDLLK
60 70 80 90 100
LCPLPAGATL AAVGGYGRGE LYPHSDVDLL ILLPRAPDGP DESAIETLVA
110 120 130 140 150
SLWDLGLEPG HSVRTLAECE TEASADITVE TALLESRWLA GSRSLMKQFE
160 170 180 190 200
TAMTARLDAR AFFRAKRVEM QQRHARYQDT PYALEPNSKE SPGGLRDLQV
210 220 230 240 250
ILWMARAAGF GRNWRAVAQA GLLTAPEARD LRRAEQAFKR LRIELHLLTR
260 270 280 290 300
RREDRLLFDL QPTLAEVYGI ATTTTRRASE LLMQRYYWAA RLVTQLNVIL
310 320 330 340 350
IQNIEERLFP RPESDARAID EEFRSLHGRL DIIREDCFER NPTLLLRAFL
360 370 380 390 400
VMQQHPGLSG MSARTLRAIW HSRHRIDAQF RRNPVNRKLF LQILQQPRGI
410 420 430 440 450
VHELRRMTML NILPRYLPVF RRIVGQMQHD LFHVYTVDQH TLAVIRNLRR
460 470 480 490 500
FTMPEHASEY PLASQVMAGL DRHWLLYVAA LFHDIAKGRG GDHSELGARD
510 520 530 540 550
ARRFAQEHGL APEDAELVEF LVRQHLLMSA VAQKRDLSDP EVINEFARQV
560 570 580 590 600
KDERHLNALY LLTVADIRGT SPKVWNAWKG KLLEDLYRLT LAALGGAQDT
610 620 630 640 650
RTVLAERKEE AARLLRLAGL RDDARDAFWQ QLDVAYFLRH DASEIAWHTR
660 670 680 690 700
HLYYQVQPDK PVVKVRPTEE GSGLQIMVYT RDTPDLFMNT CAYFDGKAFS
710 720 730 740 750
IQDARIHTTR QGWALDSFIV LPAEPLADLR AQAALVEHEL AERLRQAQGG
760 770 780 790 800
ARLADVRVFH RNRQSRVSRV FPVMPQAELH PDERSQSWRL SVTATDRPGL
810 820 830 840 850
LHALARVMAE NGVNLIMAKI MTLGDRVEDV FIISGAVLER PRTQMQFEHA

VLDALAGE
Length:858
Mass (Da):97,978
Last modified:March 7, 2006 - v1
Checksum:iDE261EA92F0D5AB7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM167904 Genomic DNA. Translation: CAJ49340.1.
RefSeqiWP_012417401.1. NC_010645.1.
YP_786250.1. NC_010645.1.

Genome annotation databases

EnsemblBacteriaiCAJ49340; CAJ49340; BAV1732.
GeneIDi6266904.
KEGGibav:BAV1732.
PATRICi21129646. VBIBorAvi43433_1744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM167904 Genomic DNA. Translation: CAJ49340.1 .
RefSeqi WP_012417401.1. NC_010645.1.
YP_786250.1. NC_010645.1.

3D structure databases

ProteinModelPortali Q2L165.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 360910.BAV1732.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAJ49340 ; CAJ49340 ; BAV1732 .
GeneIDi 6266904.
KEGGi bav:BAV1732.
PATRICi 21129646. VBIBorAvi43433_1744.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BAVI360910:GCKI-1759-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. "Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction."
    Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J., Parkhill J., Temple L.M.
    J. Bacteriol. 188:6002-6015(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 197N.

Entry informationi

Entry nameiGLND_BORA1
AccessioniPrimary (citable) accession number: Q2L165
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 7, 2006
Last modified: November 26, 2014
This is version 68 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