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Q9CNH1

- GLND_PASMU

UniProt

Q9CNH1 - GLND_PASMU

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Pasteurella multocida (strain Pm70)
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

Enzyme and pathway databases

BioCyciPMUL272843:GC8W-472-MONOMER.

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: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 enzymePRO_0000192749Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272843.PM0460.

Structurei

3D structure databases

ProteinModelPortaliQ9CNH1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini447 – 579133HDUniRule annotationAdd
BLAST
Domaini687 – 76680ACT 1UniRule annotationAdd
BLAST
Domaini793 – 86472ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 328328UridylyltransferaseAdd
BLAST
Regioni329 – 686358Uridylyl-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.
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

« Hide

        10         20         30         40         50
MLFPYFPLSE LDVSAVRTQK ENLKQFELTQ FAHYEIYDLI TNRTQFCDHL
60 70 80 90 100
LRDLWLRFGL VKDNTLTLIA VGGYGREEMF PLSDLDFLIL TSEQVEAQTE
110 120 130 140 150
QKIRQFVQFL WDCGFDVGHA VRTLSECEQA GRDNITVATN LLEARYLEGN
160 170 180 190 200
FSQFQQLDNV LQKADFWPRE AFFQAKYQER VERYQRYHNT SYNLEPDIKH
210 220 230 240 250
SPGGLRDLHL LYWIALRHTG AKNLTDILNS GFIYPQEYAQ LLESQQFLFK
260 270 280 290 300
VRFALHLILK RYDNRLLFER QIRVAELLEF VGPGNQGVEK MMKSFFQALQ
310 320 330 340 350
TISLLSDLLV KHYREHFLQT NEPVQVRLLD KEFQCVNNAI CLRQANLFVE
360 370 380 390 400
QPEQILSLFF HLTQDHQLDI HSSTLRQLHL ALEQRSGYLS ELPVARERFL
410 420 430 440 450
RLFNQPGAIA RALVPMHKYG VLKAYLPQWH HIEGLMQFDL FHCYTVDEHI
460 470 480 490 500
VRTLLKLEYF LEAESVVPHP ICSQIFSRLT DRTLLYIAAL FHDIAKGRGG
510 520 530 540 550
DHAELGAVDV AQFAQQHGFD QREIHTLTWL VEQHLLMSVT AQRRDIHDPE
560 570 580 590 600
VVLHFAEAVQ NNVRLDYLTC LTVADICATN ETLWNSWKRT LIATLYQFTT
610 620 630 640 650
QQFAQGMDCL LDHAEKIENH RQQALTLLTQ NSLLSAVQIE EIWQHCPEEY
660 670 680 690 700
FLRNTPKQIA WHTELLADNQ TELLVKISNR FSEGGTEIFV YCQDQPNLFH
710 720 730 740 750
KVVTTIGAKK FSIHDAQIIT SHDGYVFDSF IITELDGKLV KFDRRRSLEK
760 770 780 790 800
ALMQALNTSK LPTFRATDNP KLQHFHVKTE VRFLKEQRTD QTEMELFALD
810 820 830 840 850
QTGLLAKVSQ VFSELKLNLL NAKITTIGEK AEDFFILTNS EDRALTAEQR
860
QCLTQRLHEV LEPK
Length:864
Mass (Da):100,736
Last modified:June 1, 2001 - v1
Checksum:i591B1D4F2FA62F4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 83 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3