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Q2SX00

- GLND_BURTA

UniProt

Q2SX00 - GLND_BURTA

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, BTH_I2025
Organism
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
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

BioCyciBTHA271848:GJMY-2026-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:BTH_I2025
OrganismiBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Taxonomic identifieri271848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000001930: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 858858Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000022336Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi271848.BTH_I2025.

Structurei

3D structure databases

ProteinModelPortaliQ2SX00.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini444 – 550107HDAdd
BLAST
Domaini682 – 76180ACT 1Add
BLAST
Domaini790 – 85869ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 324324UridylyltransferaseUniRule annotationAdd
BLAST
Regioni325 – 681357Uridylyl-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.
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. 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.

Q2SX00-1 [UniParc]FASTAAdd to Basket

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MSASVAAPPP ALSRKAEFKA AKAELLARFQ TATNVTPLMH ALSRATDDAL    50
RRLWHECGLP ATLALVAVGG FGRGELSPHS DVDILVLLPD AHARELDERI 100
ERFIGMAWDL GLEIGSSVRT VDQCIEEASQ DVTVQTSLLE ARRIVGSTAL 150
FERFMLRYRE ALDARAFFQA KVLEMRQRHA KFQDTPYSLE PNVKESPGGL 200
RDLQTILWIA RAAGFGSSWR ELDTRGLITD REARELRRNE GFLKTLRARL 250
HVIAGRRQDI LVFDLQTQAA ESFGYRPTPA KRASEQLMRR YYWAAKAVTQ 300
LATILIQNIE AQLFPATSGV TRVLSPGRFV EKQGMLEIAA DDVFERHPDA 350
ILEAFLLYEA TRGVKGLSAR TLRALYNSRD VMNNAWRRDP RNRHTFMQIL 400
QQPEGITHAF RLMNQTSVLG RYLLNFRRIV GQMQHDLYHV YTVDQHILMV 450
LRNIRRFAVA EHAHEYPFCS QLIVNFERPW VLYVAALFHD IAKGRGGDHS 500
ALGMTDARRF CREHGIEGGD AALVVWLVQH HLTMSQVAQK QDTSDPEVIK 550
RFADLVGNER RLTALYLLTV ADIRGTSPKV WNTWKGKLLE DLYRATLAVL 600
GGAQPDAHSE LKTRQEEALA LLRLETVPPD AHRALWDQLD VGYFLRHDAA 650
DIAWQTRVLY RHVAADTAIV RARPSPVGDA LQVLVYVKDR SDLFAGICAY 700
FDRNGLSVLD ARVNTTRHGY ALDNFIVTQT ERDVQYRDIA NLVEQQLAAR 750
LAESAPLPEP SKGRLSRLSR TFPITPRVDL RADERGQYYI LSVSANDRPG 800
LLYSIARVLA EHRVGVHAAR INTLGERVED VFMLDGTGLS DNRLQIQVET 850
ELLRAIAV 858
Length:858
Mass (Da):96,880
Last modified:January 24, 2006 - v1
Checksum:i80780D220D54F576
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000086 Genomic DNA. Translation: ABC39424.1.
RefSeqiYP_442549.1. NC_007651.1.

Genome annotation databases

EnsemblBacteriaiABC39424; ABC39424; BTH_I2025.
GeneIDi3848603.
KEGGibte:BTH_I2025.
PATRICi19307090. VBIBurTha36512_4834.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000086 Genomic DNA. Translation: ABC39424.1 .
RefSeqi YP_442549.1. NC_007651.1.

3D structure databases

ProteinModelPortali Q2SX00.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 271848.BTH_I2025.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABC39424 ; ABC39424 ; BTH_I2025 .
GeneIDi 3848603.
KEGGi bte:BTH_I2025.
PATRICi 19307090. VBIBurTha36512_4834.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BTHA271848:GJMY-2026-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. "Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
    Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
    BMC Genomics 6:174-174(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Entry informationi

Entry nameiGLND_BURTA
AccessioniPrimary (citable) accession number: Q2SX00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 24, 2006
Last modified: June 11, 2014
This is version 66 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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