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Q7WJ96

- GLND_BORBR

UniProt

Q7WJ96 - GLND_BORBR

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, BB2603
Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus)
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

BioCyciBBRO257310:BB2603-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: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 enzymeUniRule annotationPRO_0000192718Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi257310.BB2603.

Structurei

3D structure databases

ProteinModelPortaliQ7WJ96.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini438 – 544107HDAdd
BLAST
Domaini676 – 76287ACT 1Add
BLAST
Domaini789 – 86577ACT 2Add
BLAST

Region

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

Q7WJ96-1 [UniParc]FASTAAdd to Basket

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MPHVDLNPLK QRMQAARAAA VAQFRQHPRP DMLLTELRRI VDQALRELVK    50
LCPLPAGATL AAVGGYGRGE LYPHSDVDLL ILLPQPPSAA DARAVEALVA 100
ALWDLGLEPG HSVRTLEDCE REARGDITVE TALLESRWLA GSRTLMKRLD 150
SAMQARLDAA VFFQAKRVEM QQRHARYQDT PYALEPNCKE SPGGLRDLQV 200
ILWMARAAGF GHSWREVAQA GLLTSSEARD LRRAEQAFKR LRIELHLLTG 250
RREDRVLFDL QPGLAAVYGI ASTATRRASE LLMQRYYWAA RLVTQLNVIL 300
VQNIEERLFP RPDSDARLID DDFRNLRERL DIVREDGFER NPTLLLRAFL 350
VMQQHPELIG MSARTLRAIW HSRHRIDAQF RRNPVNRKLF LQILQQPRGI 400
VHELRRMTML NILPRYLPVF RRIVGQMQHD LFHVYTVDQH TLAVVRNLRR 450
FTMPEHAQEY PLASQLIAGL DRHWLLYVAA LFHDIAKGRG GDHSELGARE 500
VRRFAQDHGL DPADAELVEF LVRHHLLMSA VAQKRDLSDP QVVRDFAAQV 550
GDERRLAALY LLTVADIRGT SPRVWNAWKG KLLEDLFRLT LAALGGAHAD 600
AHTVLTERKD EAARLTRLAG LRDDAREAFW NQLDIAYFLR HDASEIAWHT 650
RHLYYQVAPD EPVVRVRPTE HGEGLQVMVY TRDAPDLFVT TCGYFDAKSL 700
SVQDARVHTT RHGWALDSFI VLAPEGFADL RAQATLVEHE LAERLRDPHA 750
ARHAHAPRRL PHSHARRSRV FPVMPQAELS PDERSQSWRL SVTATDRPGL 800
LYALARVFAE HGVDLIMAKI MTLGERVEDV FIVSGSALER PRSQMQFERA 850
ILDALAGDEP RQQAA 865
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: June 11, 2014
This is version 70 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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