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A5VN81

- GLND_BRUO2

UniProt

A5VN81 - GLND_BRUO2

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, BOV_0139
Organism
Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
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
Complete GO annotation...

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

BioCyciBOVI444178:GH2V-138-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:BOV_0139
OrganismiBrucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
Taxonomic identifieri444178 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
ProteomesiUP000006383: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 934934Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_1000022329Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi444178.BOV_0139.

Structurei

3D structure databases

ProteinModelPortaliA5VN81.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini497 – 613117HD
Add
BLAST
Domaini737 – 81882ACT 1
Add
BLAST
Domaini848 – 93184ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 379379UridylyltransferaseUniRule annotation
Add
BLAST
Regioni380 – 736357Uridylyl-removingUniRule annotation
Add
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.
HOGENOMiHOG000261779.
KOiK00990.
OMAiHHLLMSV.
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. 2 hits.
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.

A5VN81-1 [UniParc]FASTAAdd to Basket

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MSAHDLKLEE IVNAETLRRK LNELADTADE SYTSLPMRKV VLQTLKDALA    50
SGRANAEDML MKDGGGTLCA KRLCYLMDTL IDILFEFATT RAYPTRNPSK 100
AENMALVAVG GYGRGGLAQG SDIDLLFLLP YKQTPWGEQV VEYTLYMLWD 150
MGLKVGHSTR NIDECIRLAR EDMTIRTALL DARFLTGDKD LFRTLEIRFE 200
EEIVKGTEPE FIQAKLAERD ARHRKAGETR YLVEPNVKEG KGGQRDLHTL 250
FWITKYFYRV KTKEELVKLG VLSRAELKLF NKAEDFLWAV RCHMHFATLK 300
AEERLSFDIQ PEIAQRLGYT AHPGQNYVER FIKHYFLVAK DVGDLTRIIC 350
AALEEQQAKH VPGFNRIFLT FSRRKRKLSD DGAFISENHR INIARPDIFR 400
QDPVNMIRLF HLADRHGLEF HPEAMQSLTR SLKLINADLR ENPEANRLFL 450
EILTSPRNPE LILRRMNESG VLGKFIPDFG KIVAMMQFNM YHHYTVDEHL 500
LRCIAVLSEI EHGELKTEHP LSNHLITTIK RDRNLLYVTL LLHDIAKGRP 550
EDHSIAGARI ARRLCPRFGL TPSETETVEW LVREHLTMSM VAQSRDLNDR 600
KTIIDFADTV QTMERLKLLL ILTVCDIKAV GPGIWNGWKG QLLRTLFYET 650
ELVLTGGFSE LSRAARDKQA REALAERLSD WPKEERDAYL ALPYTNYFLT 700
VSLDDQVRHA HFIRDADQQG RALVTMAKPH AFEAVTEITV LAPDHPRLLS 750
VITGACAAAG GNIVDAQIFT TSDGRALDTI LISREFDTDD DERRQAERVG 800
KVIEDVLSGK AHLPDMLAKR TKPKKAARAF KVEPRVEINN TLSNKFTVIE 850
VEGLDRPGLL SELTGLISDL SLDIASAHIT TFGEKVIDSF YVTDLVGHKI 900
SNATRQGNIK RKLLALLGAE NGARTNGRSP QAAA 934
Length:934
Mass (Da):105,884
Last modified:July 10, 2007 - v1
Checksum:i5CAFF6DB710AB78A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000708 Genomic DNA. Translation: ABQ61661.1.
RefSeqiYP_001258178.1. NC_009505.1.

Genome annotation databases

EnsemblBacteriaiABQ61661; ABQ61661; BOV_0139.
GeneIDi5202925.
KEGGibov:BOV_0139.
PATRICi17859996. VBIBruOvi136990_1422.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000708 Genomic DNA. Translation: ABQ61661.1 .
RefSeqi YP_001258178.1. NC_009505.1.

3D structure databases

ProteinModelPortali A5VN81.
ModBasei Search...

Protein-protein interaction databases

STRINGi 444178.BOV_0139.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ61661 ; ABQ61661 ; BOV_0139 .
GeneIDi 5202925.
KEGGi bov:BOV_0139.
PATRICi 17859996. VBIBruOvi136990_1422.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261779.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci BOVI444178:GH2V-138-MONOMER.

Miscellaneous databases

PROi A5VN81.

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. 2 hits.
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. Paulsen I.
    Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25840 / 63/290 / NCTC 10512.

Entry informationi

Entry nameiGLND_BRUO2
AccessioniPrimary (citable) accession number: A5VN81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: June 11, 2014
This is version 52 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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