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Q7VYD2

- GLND_BORPE

UniProt

Q7VYD2 - GLND_BORPE

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
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

BioCyciBPER257313:BP1417-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:BP1417
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
ProteomesiUP000002676: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 865865Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192720Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi257313.BP1417.

Structurei

3D structure databases

ProteinModelPortaliQ7VYD2.
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.

Q7VYD2 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPHVDLNPLK QRMQAARAAA VAQFRQHPRP DMLLTELRRI VDQALRELVK
60 70 80 90 100
LCPLPAGATL AAVGSYGRGE LYPHSDVDLL ILLPQPPSAA DARAVEALVA
110 120 130 140 150
ALWDLGLEPG HSVRTLEDCE REARGDITVE TALLESRWLA GSRTLMKRLD
160 170 180 190 200
SAMQARLDAA VFFQAKRVEM QQRHAHYQDT 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 DPTDAELVEF 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):98,524
Last modified:October 1, 2003 - v1
Checksum:iD8E17E5527129A45
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640415 Genomic DNA. Translation: CAE41707.1.
RefSeqiNP_880159.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaiCAE41707; CAE41707; BP1417.
GeneIDi2667683.
KEGGibpe:BP1417.
PATRICi21156046. VBIBorPer7866_1519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BX640415 Genomic DNA. Translation: CAE41707.1 .
RefSeqi NP_880159.1. NC_002929.2.

3D structure databases

ProteinModelPortali Q7VYD2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 257313.BP1417.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAE41707 ; CAE41707 ; BP1417 .
GeneIDi 2667683.
KEGGi bpe:BP1417.
PATRICi 21156046. VBIBorPer7866_1519.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BPER257313:BP1417-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: Tohama I / ATCC BAA-589 / NCTC 13251.

Entry informationi

Entry nameiGLND_BORPE
AccessioniPrimary (citable) accession number: Q7VYD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: October 1, 2003
Last modified: October 29, 2014
This is version 71 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