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Q62JC2

- GLND_BURMA

UniProt

Q62JC2 - GLND_BURMA

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Burkholderia mallei (strain ATCC 23344)
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

Mg2+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

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:BMA1557
OrganismiBurkholderia mallei (strain ATCC 23344)
Taxonomic identifieri243160 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group
ProteomesiUP000006693: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 858858Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192725Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi243160.BMA1557.

Structurei

3D structure databases

ProteinModelPortaliQ62JC2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini444 – 550107HDUniRule annotationAdd
BLAST
Domaini682 – 76180ACT 1UniRule annotationAdd
BLAST
Domaini790 – 85869ACT 2UniRule annotationAdd
BLAST

Region

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

Q62JC2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSASVAEPPP ALSRKAEFKA AKAELLARFK SANHVTPLMH ALSRATDDAL
60 70 80 90 100
RSLWQECGLP ATLALVAVGG FGRGELSPHS DVDILVLLPD AHASELDERI
110 120 130 140 150
ERFIGMAWDL GLEIGSSVRT VDQCIEEASH DVTVQTSLLE ARRIVGSTAL
160 170 180 190 200
FERFMLRYRE ALDARAFFQA KVLEMRQRHA KFQNTPYSLE PNVKESPGGL
210 220 230 240 250
RDLQTILWIA RAAGFGSSWR ELDTRGLITD REARELRRNE GFLKTLRARL
260 270 280 290 300
HVIAGRRQDI LVFDLQTQAA ESFGYQPTSA KRASEQLMRR YYWAAKAVTQ
310 320 330 340 350
LATILIQNIE AQLFPATSGV TRVLSPGRFV EKQGMLEIAA DDVFERHPDA
360 370 380 390 400
ILEAFLLYEA TRGVKGLSAR TLRALYNSRD VMNNAWRRDP RNRHTFMQIL
410 420 430 440 450
QQPEGITHAF RLMNQTSVLG RYLLNFRRIV GQMQHDLYHV YTVDQHILMV
460 470 480 490 500
LRNIRRFAVA EHAHEYPFCS QLIVNFERPW VLYVAALFHD IAKGRGGDHS
510 520 530 540 550
ALGMADARRF CREHGIEGDD AALVVWLVQH HLTMSQVAQK QDTSDPVVIK
560 570 580 590 600
RFAELVGSER RLTALYLLTV ADIRGTSPKV WNTWKGKLLE DLYRATLAVL
610 620 630 640 650
GGAQPDAHSE LKTRQEEALA LLRLETVPPD AHRALWDQLD VGYFLRHDAA
660 670 680 690 700
DIAWQTRVLY RHVAADTAIV RARPSPVGDA LQVLVYVKDR SDLFAGICAY
710 720 730 740 750
FDRNGLSVLD ARVNTTRHGY ALDNFIVTQT EHDVQYRDIA NLVEQQLAAR
760 770 780 790 800
LAESAPLPEP SKGRLSRLSR TFPITPRVDL RADERGQYYI LSVSANDRPG
810 820 830 840 850
LLYSIARVLA EHRVGVHAAR INTLGERVED VFMLDGTGLS DNRLQIQVET

ELLRAIAV
Length:858
Mass (Da):96,749
Last modified:October 25, 2004 - v1
Checksum:i6089EDA7B3B68530
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000010 Genomic DNA. Translation: AAU47757.1.
RefSeqiYP_103197.1. NC_006348.1.

Genome annotation databases

EnsemblBacteriaiAAU47757; AAU47757; BMA1557.
GeneIDi3088304.
KEGGibma:BMA1557.
PATRICi19118172. VBIBurMal55007_1603.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000010 Genomic DNA. Translation: AAU47757.1 .
RefSeqi YP_103197.1. NC_006348.1.

3D structure databases

ProteinModelPortali Q62JC2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243160.BMA1557.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAU47757 ; AAU47757 ; BMA1557 .
GeneIDi 3088304.
KEGGi bma:BMA1557.
PATRICi 19118172. VBIBurMal55007_1603.

Phylogenomic databases

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

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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 23344.

Entry informationi

Entry nameiGLND_BURMA
AccessioniPrimary (citable) accession number: Q62JC2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: October 25, 2004
Last modified: November 26, 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3