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Q7WJ96

- GLND_BORBR

UniProt

Q7WJ96 - GLND_BORBR

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
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

Magnesium.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

BioCyciBBRO257310:BB2603-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:BB2603
OrganismiBordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
Taxonomic identifieri257310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000001027: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 865865Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192718Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi257310.BB2603.

Structurei

3D structure databases

ProteinModelPortaliQ7WJ96.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini438 – 544107HDUniRule annotationAdd
BLAST
Domaini676 – 76287ACT 1UniRule annotationAdd
BLAST
Domaini789 – 86577ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 318318UridylyltransferaseAdd
BLAST
Regioni319 – 675357Uridylyl-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.

Q7WJ96-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPHVDLNPLK QRMQAARAAA VAQFRQHPRP DMLLTELRRI VDQALRELVK
60 70 80 90 100
LCPLPAGATL AAVGGYGRGE LYPHSDVDLL ILLPQPPSAA DARAVEALVA
110 120 130 140 150
ALWDLGLEPG HSVRTLEDCE REARGDITVE TALLESRWLA GSRTLMKRLD
160 170 180 190 200
SAMQARLDAA VFFQAKRVEM QQRHARYQDT PYALEPNCKE SPGGLRDLQV
210 220 230 240 250
ILWMARAAGF GHSWREVAQA GLLTSSEARD LRRAEQAFKR LRIELHLLTG
260 270 280 290 300
RREDRVLFDL QPGLAAVYGI ASTATRRASE LLMQRYYWAA RLVTQLNVIL
310 320 330 340 350
VQNIEERLFP RPDSDARLID DDFRNLRERL DIVREDGFER NPTLLLRAFL
360 370 380 390 400
VMQQHPELIG MSARTLRAIW HSRHRIDAQF RRNPVNRKLF LQILQQPRGI
410 420 430 440 450
VHELRRMTML NILPRYLPVF RRIVGQMQHD LFHVYTVDQH TLAVVRNLRR
460 470 480 490 500
FTMPEHAQEY PLASQLIAGL DRHWLLYVAA LFHDIAKGRG GDHSELGARE
510 520 530 540 550
VRRFAQDHGL DPADAELVEF LVRHHLLMSA VAQKRDLSDP QVVRDFAAQV
560 570 580 590 600
GDERRLAALY LLTVADIRGT SPRVWNAWKG KLLEDLFRLT LAALGGAHAD
610 620 630 640 650
AHTVLTERKD EAARLTRLAG LRDDAREAFW NQLDIAYFLR HDASEIAWHT
660 670 680 690 700
RHLYYQVAPD EPVVRVRPTE HGEGLQVMVY TRDAPDLFVT TCGYFDAKSL
710 720 730 740 750
SVQDARVHTT RHGWALDSFI VLAPEGFADL RAQATLVEHE LAERLRDPHA
760 770 780 790 800
ARHAHAPRRL PHSHARRSRV FPVMPQAELS PDERSQSWRL SVTATDRPGL
810 820 830 840 850
LYALARVFAE HGVDLIMAKI MTLGERVEDV FIVSGSALER PRSQMQFERA
860
ILDALAGDEP RQQAA
Length:865
Mass (Da):98,483
Last modified:October 1, 2003 - v1
Checksum:iBCD00076B7F9DB79
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640444 Genomic DNA. Translation: CAE33096.1.
RefSeqiNP_889140.1. NC_002927.3.

Genome annotation databases

EnsemblBacteriaiCAE33096; CAE33096; BB2603.
GeneIDi2662666.
KEGGibbr:BB2603.
PATRICi21138539. VBIBorBro124907_2638.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640444 Genomic DNA. Translation: CAE33096.1 .
RefSeqi NP_889140.1. NC_002927.3.

3D structure databases

ProteinModelPortali Q7WJ96.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257310.BB2603.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE33096 ; CAE33096 ; BB2603 .
GeneIDi 2662666.
KEGGi bbr:BB2603.
PATRICi 21138539. VBIBorBro124907_2638.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BBRO257310:BB2603-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. "Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
    Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S.
    , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
    Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-588 / NCTC 13252 / RB50.

Entry informationi

Entry nameiGLND_BORBR
AccessioniPrimary (citable) accession number: Q7WJ96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: October 1, 2003
Last modified: October 29, 2014
This is version 72 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