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Q2L165

- GLND_BORA1

UniProt

Q2L165 - GLND_BORA1

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, BAV1732
Organism
Bordetella avium (strain 197N)
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

BioCyciBAVI360910:GCKI-1759-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: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 enzymeUniRule annotationPRO_1000022326Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi360910.BAV1732.

Structurei

3D structure databases

ProteinModelPortaliQ2L165.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini438 – 550113HDAdd
BLAST
Domaini675 – 75682ACT 1Add
BLAST
Domaini789 – 85870ACT 2Add
BLAST

Region

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

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MNPTDLHPIK ERMQAARAAA IADFRQHLRP DPLLSELRRI VDQALRDLLK    50
LCPLPAGATL AAVGGYGRGE LYPHSDVDLL ILLPRAPDGP DESAIETLVA 100
SLWDLGLEPG HSVRTLAECE TEASADITVE TALLESRWLA GSRSLMKQFE 150
TAMTARLDAR AFFRAKRVEM QQRHARYQDT PYALEPNSKE SPGGLRDLQV 200
ILWMARAAGF GRNWRAVAQA GLLTAPEARD LRRAEQAFKR LRIELHLLTR 250
RREDRLLFDL QPTLAEVYGI ATTTTRRASE LLMQRYYWAA RLVTQLNVIL 300
IQNIEERLFP RPESDARAID EEFRSLHGRL DIIREDCFER NPTLLLRAFL 350
VMQQHPGLSG MSARTLRAIW HSRHRIDAQF RRNPVNRKLF LQILQQPRGI 400
VHELRRMTML NILPRYLPVF RRIVGQMQHD LFHVYTVDQH TLAVIRNLRR 450
FTMPEHASEY PLASQVMAGL DRHWLLYVAA LFHDIAKGRG GDHSELGARD 500
ARRFAQEHGL APEDAELVEF LVRQHLLMSA VAQKRDLSDP EVINEFARQV 550
KDERHLNALY LLTVADIRGT SPKVWNAWKG KLLEDLYRLT LAALGGAQDT 600
RTVLAERKEE AARLLRLAGL RDDARDAFWQ QLDVAYFLRH DASEIAWHTR 650
HLYYQVQPDK PVVKVRPTEE GSGLQIMVYT RDTPDLFMNT CAYFDGKAFS 700
IQDARIHTTR QGWALDSFIV LPAEPLADLR AQAALVEHEL AERLRQAQGG 750
ARLADVRVFH RNRQSRVSRV FPVMPQAELH PDERSQSWRL SVTATDRPGL 800
LHALARVMAE NGVNLIMAKI MTLGDRVEDV FIISGAVLER PRTQMQFEHA 850
VLDALAGE 858
Length:858
Mass (Da):97,978
Last modified:March 7, 2006 - v1
Checksum:iDE261EA92F0D5AB7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM167904 Genomic DNA. Translation: CAJ49340.1.
RefSeqiYP_786250.1. NC_010645.1.

Genome annotation databases

GeneIDi6266904.
KEGGibav:BAV1732.
PATRICi21129646. VBIBorAvi43433_1744.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM167904 Genomic DNA. Translation: CAJ49340.1 .
RefSeqi 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

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: June 11, 2014
This is version 65 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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