SubmitCancel

Skip Header

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

Q9Z9H0

- GLND_PSEAE

UniProt

Q9Z9H0 - GLND_PSEAE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Bifunctional uridylyltransferase/uridylyl-removing enzyme
Gene
glnD, PA3658
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
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

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

Organism-specific databases

PseudoCAPiPA3658.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 900900Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
PRO_0000192752Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi208964.PA3658.

Structurei

3D structure databases

ProteinModelPortaliQ9Z9H0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini463 – 569107HD
Add
BLAST
Domaini706 – 78984ACT 1
Add
BLAST
Domaini816 – 89176ACT 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 342342UridylyltransferaseUniRule annotation
Add
BLAST
Regioni343 – 705363Uridylyl-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.
OMAiHHLLMSV.
OrthoDBiEOG6CCH44.
PhylomeDBiQ9Z9H0.

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.

Q9Z9H0-1 [UniParc]FASTAAdd to Basket

« Hide

MPQVDPELFD RGQFQAELAL KSSPIAAFKK AIRQFREVLD NRFNSGRDIR    50
RLIEDRAWCV DQILQQAWQR FDWGDDADIA LVAVGGYGRG ELHPYSDVDL 100
LILLDSEDQE SFREPIEGFL TLLWDIGLEV GQSVRSVQQC AEEARADLTV 150
ITTLMECRTI CGPDSLRQRM LQVTGSAHMW PSKEFFLAKR HEQQRRHAKY 200
NDTEYNLEPN VKGSPGGLRD IQTILWMARR QFGSLNLHAL VREGFLVESE 250
CSMLASSQEF LWRVRYALHM LAGRAEDRLL FDHQRSIARL FGYEDNDVKL 300
AVERFMQKYY RVVMAISELN DLIIQHFEEV ILPCEQPVQI QPLNSRFQLR 350
DGYIEVTHPN VFKRTPFALL EIFVLMAQHP EIKGVRADTI RLLRDSRHLI 400
DDEFRHDIRN TSLFIELFKS SQGIHRNLRR MNRYGILGRY LPEFGHIIGQ 450
MQHDLFHIYT VDAHTLNLIK HLRKLNRPEM AEKYPLASKI IDRLPKPELI 500
YIAGLYHDIA KGRGGDHSEL GAVDAEAFCQ SHQLPLWDTQ LVSWLVQNHL 550
VMSTTAQRKD LSDPQVIFDF AQLVGDQTHL DYLYVLTVAD INATNPTLWN 600
SWRASLLRQL YTETKRALRR GLENPVDREE QIRQTQTAAL DQLVRNGIDQ 650
DDAEQLWSQL GDDYFLRHTA GDVAWHTEAI LQHPDDGTPL VLIKETTQRE 700
FESGSQIFIY AADQHDFFAV TVAAMDQLNL SIQDARIITS TSQFTLDTYI 750
VLDADGDSIG NNPERIAEIR EGLIDALKNP DDYPTIIQRR VPRQLKHFAF 800
APQVTISTDA LRQVSVLEVI APDRPGLLAR IGGIFLDFDL SVQNAKIATL 850
GERVEDVFYI TDARNQPLAD PDLCKRLQAA LVEQLSQDNG RDTLPTRINF 900
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.

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB024601 Genomic DNA. Translation: BAA75913.1. Frameshift.
AE004091 Genomic DNA. Translation: AAG07046.1.
PIRiE83189.
RefSeqiNP_252348.1. NC_002516.2.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB024601 Genomic DNA. Translation: BAA75913.1 . Frameshift.
AE004091 Genomic DNA. Translation: AAG07046.1 .
PIRi E83189.
RefSeqi NP_252348.1. NC_002516.2.

3D structure databases

ProteinModelPortali Q9Z9H0.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208964.PA3658.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG07046 ; AAG07046 ; PA3658 .
GeneIDi 880565.
KEGGi pae:PA3658.
PATRICi 19841939. VBIPseAer58763_3827.

Organism-specific databases

PseudoCAPi PA3658.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.
PhylomeDBi Q9Z9H0.

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

« 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 9, 2014
This is version 97 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