Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed-Annotation score: 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

GO - Biological processi

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:PA3658
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA3658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192752Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi208964.PA3658.

Structurei

3D structure databases

ProteinModelPortaliQ9Z9H0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini463 – 569107HDUniRule annotationAdd
BLAST
Domaini706 – 78984ACT 1UniRule annotationAdd
BLAST
Domaini816 – 89176ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 342342UridylyltransferaseAdd
BLAST
Regioni343 – 705363Uridylyl-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.
InParanoidiQ9Z9H0.
KOiK00990.
OMAiHTLFWIA.
OrthoDBiEOG6CCH44.
PhylomeDBiQ9Z9H0.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[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.

Q9Z9H0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQVDPELFD RGQFQAELAL KSSPIAAFKK AIRQFREVLD NRFNSGRDIR
60 70 80 90 100
RLIEDRAWCV DQILQQAWQR FDWGDDADIA LVAVGGYGRG ELHPYSDVDL
110 120 130 140 150
LILLDSEDQE SFREPIEGFL TLLWDIGLEV GQSVRSVQQC AEEARADLTV
160 170 180 190 200
ITTLMECRTI CGPDSLRQRM LQVTGSAHMW PSKEFFLAKR HEQQRRHAKY
210 220 230 240 250
NDTEYNLEPN VKGSPGGLRD IQTILWMARR QFGSLNLHAL VREGFLVESE
260 270 280 290 300
CSMLASSQEF LWRVRYALHM LAGRAEDRLL FDHQRSIARL FGYEDNDVKL
310 320 330 340 350
AVERFMQKYY RVVMAISELN DLIIQHFEEV ILPCEQPVQI QPLNSRFQLR
360 370 380 390 400
DGYIEVTHPN VFKRTPFALL EIFVLMAQHP EIKGVRADTI RLLRDSRHLI
410 420 430 440 450
DDEFRHDIRN TSLFIELFKS SQGIHRNLRR MNRYGILGRY LPEFGHIIGQ
460 470 480 490 500
MQHDLFHIYT VDAHTLNLIK HLRKLNRPEM AEKYPLASKI IDRLPKPELI
510 520 530 540 550
YIAGLYHDIA KGRGGDHSEL GAVDAEAFCQ SHQLPLWDTQ LVSWLVQNHL
560 570 580 590 600
VMSTTAQRKD LSDPQVIFDF AQLVGDQTHL DYLYVLTVAD INATNPTLWN
610 620 630 640 650
SWRASLLRQL YTETKRALRR GLENPVDREE QIRQTQTAAL DQLVRNGIDQ
660 670 680 690 700
DDAEQLWSQL GDDYFLRHTA GDVAWHTEAI LQHPDDGTPL VLIKETTQRE
710 720 730 740 750
FESGSQIFIY AADQHDFFAV TVAAMDQLNL SIQDARIITS TSQFTLDTYI
760 770 780 790 800
VLDADGDSIG NNPERIAEIR EGLIDALKNP DDYPTIIQRR VPRQLKHFAF
810 820 830 840 850
APQVTISTDA LRQVSVLEVI APDRPGLLAR IGGIFLDFDL SVQNAKIATL
860 870 880 890 900
GERVEDVFYI TDARNQPLAD PDLCKRLQAA LVEQLSQDNG RDTLPTRINF
Length:900
Mass (Da):103,404
Last modified:December 8, 2000 - v2
Checksum:i7C71F31EC284E836
GO

Sequence cautioni

The sequence BAA75913.1 differs from that shown. Reason: Frameshift at position 285. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti811 – 8111L → V in BAA75913 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024601 Genomic DNA. Translation: BAA75913.1. Frameshift.
AE004091 Genomic DNA. Translation: AAG07046.1.
PIRiE83189.
RefSeqiNP_252348.1. NC_002516.2.
WP_003113862.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG07046; AAG07046; PA3658.
GeneIDi880565.
KEGGipae:PA3658.
PATRICi19841939. VBIPseAer58763_3827.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB024601 Genomic DNA. Translation: BAA75913.1. Frameshift.
AE004091 Genomic DNA. Translation: AAG07046.1.
PIRiE83189.
RefSeqiNP_252348.1. NC_002516.2.
WP_003113862.1. NC_002516.2.

3D structure databases

ProteinModelPortaliQ9Z9H0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi208964.PA3658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG07046; AAG07046; PA3658.
GeneIDi880565.
KEGGipae:PA3658.
PATRICi19841939. VBIPseAer58763_3827.

Organism-specific databases

PseudoCAPiPA3658.

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
InParanoidiQ9Z9H0.
KOiK00990.
OMAiHTLFWIA.
OrthoDBiEOG6CCH44.
PhylomeDBiQ9Z9H0.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Nashimoto H.
    Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Entry informationi

Entry nameiGLND_PSEAE
AccessioniPrimary (citable) accession number: Q9Z9H0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 8, 2000
Last modified: July 22, 2015
This is version 104 of the entry and version 2 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.