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Q9CNH1

- GLND_PASMU

UniProt

Q9CNH1 - GLND_PASMU

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, PM0460
Organism
Pasteurella multocida (strain Pm70)
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

BioCyciPMUL272843:GC8W-472-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:PM0460
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
ProteomesiUP000000809: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 864864Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_0000192749Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272843.PM0460.

Structurei

3D structure databases

ProteinModelPortaliQ9CNH1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini447 – 579133HDAdd
BLAST
Domaini687 – 76680ACT 1Add
BLAST
Domaini793 – 86472ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 328328UridylyltransferaseUniRule annotationAdd
BLAST
Regioni329 – 686358Uridylyl-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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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.

Q9CNH1-1 [UniParc]FASTAAdd to Basket

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MLFPYFPLSE LDVSAVRTQK ENLKQFELTQ FAHYEIYDLI TNRTQFCDHL    50
LRDLWLRFGL VKDNTLTLIA VGGYGREEMF PLSDLDFLIL TSEQVEAQTE 100
QKIRQFVQFL WDCGFDVGHA VRTLSECEQA GRDNITVATN LLEARYLEGN 150
FSQFQQLDNV LQKADFWPRE AFFQAKYQER VERYQRYHNT SYNLEPDIKH 200
SPGGLRDLHL LYWIALRHTG AKNLTDILNS GFIYPQEYAQ LLESQQFLFK 250
VRFALHLILK RYDNRLLFER QIRVAELLEF VGPGNQGVEK MMKSFFQALQ 300
TISLLSDLLV KHYREHFLQT NEPVQVRLLD KEFQCVNNAI CLRQANLFVE 350
QPEQILSLFF HLTQDHQLDI HSSTLRQLHL ALEQRSGYLS ELPVARERFL 400
RLFNQPGAIA RALVPMHKYG VLKAYLPQWH HIEGLMQFDL FHCYTVDEHI 450
VRTLLKLEYF LEAESVVPHP ICSQIFSRLT DRTLLYIAAL FHDIAKGRGG 500
DHAELGAVDV AQFAQQHGFD QREIHTLTWL VEQHLLMSVT AQRRDIHDPE 550
VVLHFAEAVQ NNVRLDYLTC LTVADICATN ETLWNSWKRT LIATLYQFTT 600
QQFAQGMDCL LDHAEKIENH RQQALTLLTQ NSLLSAVQIE EIWQHCPEEY 650
FLRNTPKQIA WHTELLADNQ TELLVKISNR FSEGGTEIFV YCQDQPNLFH 700
KVVTTIGAKK FSIHDAQIIT SHDGYVFDSF IITELDGKLV KFDRRRSLEK 750
ALMQALNTSK LPTFRATDNP KLQHFHVKTE VRFLKEQRTD QTEMELFALD 800
QTGLLAKVSQ VFSELKLNLL NAKITTIGEK AEDFFILTNS EDRALTAEQR 850
QCLTQRLHEV LEPK 864
Length:864
Mass (Da):100,736
Last modified:June 1, 2001 - v1
Checksum:i591B1D4F2FA62F4E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004439 Genomic DNA. Translation: AAK02544.1.
RefSeqiNP_245397.1. NC_002663.1.
WP_010906658.1. NC_002663.1.

Genome annotation databases

EnsemblBacteriaiAAK02544; AAK02544; PM0460.
GeneIDi1243807.
KEGGipmu:PM0460.
PATRICi22870096. VBIPasMul88067_0472.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004439 Genomic DNA. Translation: AAK02544.1 .
RefSeqi NP_245397.1. NC_002663.1.
WP_010906658.1. NC_002663.1.

3D structure databases

ProteinModelPortali Q9CNH1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272843.PM0460.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK02544 ; AAK02544 ; PM0460 .
GeneIDi 1243807.
KEGGi pmu:PM0460.
PATRICi 22870096. VBIPasMul88067_0472.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci PMUL272843:GC8W-472-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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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: Pm70.

Entry informationi

Entry nameiGLND_PASMU
AccessioniPrimary (citable) accession number: Q9CNH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 80 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