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A2SB69

- GLND_BURM9

UniProt

A2SB69 - GLND_BURM9

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Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, BMA10229_A3252
Organism
Burkholderia mallei (strain NCTC 10229)
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

BioCyciBMAL412022:GJI8-3251-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:BMA10229_A3252
OrganismiBurkholderia mallei (strain NCTC 10229)
Taxonomic identifieri412022 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000002283: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 858858Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_1000022332Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi412022.BMA10229_A3252.

Structurei

3D structure databases

ProteinModelPortaliA2SB69.

Family & Domainsi

Domains and Repeats

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

Region

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

A2SB69-1 [UniParc]FASTAAdd to Basket

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MSASVAEPPP ALSRKAEFKA AKAELLARFK SANHVTPLMH ALSRATDDAL    50
RSLWQECGLP ATLALVAVGG FGRGELSPHS DVDILVLLPD AHASELDERI 100
ERFIGMAWDL GLEIGSSVRT VDQCIEEASH DVTVQTSLLE ARRIVGSTAL 150
FERFMLRYRE ALDARAFFQA KVLEMRQRHA KFQDTPYSLE PNVKESPGGL 200
RDLQTILWIA RAAGFGSSWR ELDTRGLITD REARELRRNE GFLKTLRARL 250
HVIAGRRQDI LVFDLQTQAA ESFGYQPTSA 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
ALGMADARRF CREHGIEGDD AALVVWLVQH HLTMSQVAQK QDTSDPVVIK 550
RFAELVGSER RLTALYLLTV ADIRGTSPKV WNTWKGKLLE DLYRATLAVL 600
GGAQPDAHSE LKTRQEEALA LLRLETVPPD AHRALWDQLD VGYFLRHDAA 650
DIAWQTRVLY RHVAADTAIV RARPSPVGDA LQVLVYVKDR SDLFAGICAY 700
FDRNGLSVLD ARVNTTRHGY ALDNFIVTQT EHDVQYRDIA NLVEQQLAAR 750
LAESAPLPEP SKGRLSRLSR TFPITPRVDL RADERGQYYI LSVSANDRPG 800
LLYSIARVLA EHRVGVHAAR INTLGERVED VFMLDGTGLS DNRLQIQVET 850
ELLRAIAV 858
Length:858
Mass (Da):96,750
Last modified:March 6, 2007 - v1
Checksum:iE71C618DBA6FE7F4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000546 Genomic DNA. Translation: ABN00892.1.
RefSeqiYP_001029188.1. NC_008836.1.

Genome annotation databases

EnsemblBacteriaiABN00892; ABN00892; BMA10229_A3252.
GeneIDi4793516.
KEGGibml:BMA10229_A3252.
PATRICi19137520. VBIBurMal46188_5445.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000546 Genomic DNA. Translation: ABN00892.1 .
RefSeqi YP_001029188.1. NC_008836.1.

3D structure databases

ProteinModelPortali A2SB69.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 412022.BMA10229_A3252.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABN00892 ; ABN00892 ; BMA10229_A3252 .
GeneIDi 4793516.
KEGGi bml:BMA10229_A3252.
PATRICi 19137520. VBIBurMal46188_5445.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci BMAL412022:GJI8-3251-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. DeShazer D., Woods D.E., Nierman W.C.
    Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 10229.

Entry informationi

Entry nameiGLND_BURM9
AccessioniPrimary (citable) accession number: A2SB69
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: June 11, 2014
This is version 55 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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