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Q4ZWT0 (GLND_PSEU2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:

  1. [Protein-PII] uridylyltransferase
    Short name=PII uridylyltransferase
    Short name=UTase
    EC=2.7.7.59
  2. [Protein-PII]-UMP uridylyl-removing enzyme
    Short name=UR
    EC=3.1.4.-
Gene names
Name:glnD
Ordered Locus Names:Psyr_1341
OrganismPseudomonas syringae pv. syringae (strain B728a) [Complete proteome] [HAMAP]
Taxonomic identifier205918 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonasPseudomonas syringae

Protein attributes

Sequence length898 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00277

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP-Rule MF_00277

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. HAMAP-Rule MF_00277

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00277

Enzyme regulation

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity. HAMAP-Rule MF_00277

Domain

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. HAMAP-Rule MF_00277

Sequence similarities

Belongs to the GlnD family.

Contains 2 ACT domains.

Contains 1 HD domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 898898Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192755

Regions

Domain463 – 567105HD
Domain705 – 78884ACT 1
Domain815 – 89177ACT 2
Region1 – 341341Uridylyltransferase HAMAP-Rule MF_00277
Region342 – 704363Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q4ZWT0 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 29A660560C867427

FASTA898102,870
        10         20         30         40         50         60 
MPQVDPDLFD RGQFQAELAL KASPIAAFKK AIRRARDVLD ERFRSGRDIR RLIEDRAWFV 

        70         80         90        100        110        120 
DNILQKAWDQ FEWSEDADIA LLAVGGYGRG ELHPYSDIDL LILLDSDDHE VFREPIERFL 

       130        140        150        160        170        180 
TLLWDIGLEV GQSVRSVNEC AQEGRADLTV ITNLMESRTI AGPEHLRQRM LEVTSTEHMW 

       190        200        210        220        230        240 
PSKEFFLAKH AEQKKRHHKY NDTEYNLEPN VKGSPGGLRD IQTILWVARR QYGTLNLHAL 

       250        260        270        280        290        300 
AGEGFLLGSE NALLASSQEF LWKVRYALHM LAGRSEDRLL FDYQVRIAGL LGYEDNDAKL 

       310        320        330        340        350        360 
AIERFMQKYY RVVMSIAELS DLIIQHFEEV ILSDDSGTPQ PINSRFQLHD GYIEATHQNV 

       370        380        390        400        410        420 
FKRTPFAMIE IFVLMAQHPE IKGVRADTIR LLREHRHLIN DEFRNDIRNT SLFIELFKCE 

       430        440        450        460        470        480 
IGIHRNLRRM NRYGILGLYL PEFGHIVGQM QHDLFHIYTV DAHTLNLIKH LRKLQYTEVS 

       490        500        510        520        530        540 
EKFPLASKIM GRLPKPELIY LAGLYHDIGK GRGGDHSELG AIDAQAFGAR HHLPAWDTRL 

       550        560        570        580        590        600 
IVWLVSNHLV MSTTAQRKDL SDPQVIHDFA QFVGDEVHLD YLYVLTVADI NATNPTLWNS 

       610        620        630        640        650        660 
WRASLLRQLY TETKRALRRG LENPVDREEQ IRRTQTAALD ILVRNGTDPD DVEQLWSALG 

       670        680        690        700        710        720 
DDYFLRHTAG DVAWHSDAIL QQPADGGPLV LIKETTQREF EGGTQIFIYA PDQHDFFAVT 

       730        740        750        760        770        780 
VAAMDQLNLN IHDARIITSS SKFTLDTYIV LDHEGGSIGN NPERIQDIRE GLTEALRNPD 

       790        800        810        820        830        840 
DYPTIIKRRV PRQLKHFAFA PQVTIHNDAQ RPVTVLELLA PDRPGLLARI GKIFLEFDLS 

       850        860        870        880        890 
LQNAKIATLG ERVEDVFFIT DANNHPLSDP QLCRQLQDAI VKQLSVNSEP GNDLRISI 

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References

[1]"Comparison of the complete genome sequences of Pseudomonas syringae pv. syringae B728a and pv. tomato DC3000."
Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A., Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S., Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M., Kyrpides N.C., Ivanova N., Lindow S.E.
Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: B728a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000075 Genomic DNA. Translation: AAY36392.1.
RefSeqYP_234430.1. NC_007005.1.

3D structure databases

ProteinModelPortalQ4ZWT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205918.Psyr_1341.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY36392; AAY36392; Psyr_1341.
GeneID3366836.
KEGGpsb:Psyr_1341.
PATRIC19983173. VBIPseSyr42314_1374.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK00275.

Enzyme and pathway databases

BioCycPSYR205918:GJ94-1361-MONOMER.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFPIRSF006288. PII_uridyltransf. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR01693. UTase_glnD. 1 hit.
PROSITEPS51671. ACT. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLND_PSEU2
AccessionPrimary (citable) accession number: Q4ZWT0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: June 7, 2005
Last modified: February 19, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families