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Q5F8H5 (GLND_NEIG1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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:NGO0798
OrganismNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090) [Reference proteome] [HAMAP]
Taxonomic identifier242231 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length852 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 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192746

Regions

Domain437 – 539103HD
Domain673 – 75785ACT 1
Domain785 – 85268ACT 2
Region1 – 318318Uridylyltransferase HAMAP-Rule MF_00277
Region319 – 672354Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q5F8H5 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 446EC476F5205885

FASTA85296,964
        10         20         30         40         50         60 
MPENLSSALE TFKQQRNAAE AHYLKANRVS VFFREYTAAV ETLLAALWAE HFQNSALCLM 

        70         80         90        100        110        120 
AVGGFGRGEP YPCSDVDLAV VSPAPLSDGI QEQIARFIQT LWDCKLMPSV KSGSVDELCE 

       130        140        150        160        170        180 
SVRDDITGDT AFLEARFLFG NRQTADELAE KMNVQRNVAA FIEAKLVEME HRHAKSQGSG 

       190        200        210        220        230        240 
AVLEPNIKSC PGGLRDIHTL LWIAKAQGLA ANLPDLLKQR ILTRAEAGML SHGYRRLAHI 

       250        260        270        280        290        300 
RIRLHLNAKR AEDRLLFDLQ PQVAESMGYQ DENRRRQSEE LMRVFYRAVK TVKQLGGILT 

       310        320        330        340        350        360 
PMLRSRVSST PVRVTLRIDD DYIQVNNQIA ARHTDIFFRR PEHIFKIVEI MQQRNDITAL 

       370        380        390        400        410        420 
EPQTLRAWWG ATRKINRSFY QNSENRRRFA GFFRSGNGLT QTLRFLNLYG VLGRYLPAWE 

       430        440        450        460        470        480 
KIVGLLQHDL FHIYPVDDHI LAVVRNVRRL ALDMHSHELP YASALMQSFE KQDILYLAAF 

       490        500        510        520        530        540 
FHDIAKGRGG DHAVQGIADA RQFAADHFLT EEESDLLAWL VENHLLMSAV AQKEDIQDPG 

       550        560        570        580        590        600 
VLDAFCKRVQ THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RCLAGNDGNP 

       610        620        630        640        650        660 
HALFGRRRQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA NLVHDFEPPI 

       670        680        690        700        710        720 
VRSRILPQSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL AARAFITEHD YILDTFIVQI 

       730        740        750        760        770        780 
PSQHAPEDYP DIQSALEAEL NSFIHGHTVA ETQSCNRRIS RRSRYMPIAP SITITPEEDY 

       790        800        810        820        830        840 
PDRYSVEITA VNRPFLLADM AEVFFAHNVS LRYAKISTLD ERVEDSFTVF SPDLKNPKIQ 

       850 
SSLKQALLEQ LA 

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References

[1]"The complete genome sequence of Neisseria gonorrhoeae."
Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H. expand/collapse author list , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700825 / FA 1090.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004969 Genomic DNA. Translation: AAW89512.1.
RefSeqYP_207924.1. NC_002946.2.

3D structure databases

ProteinModelPortalQ5F8H5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING242231.NGO0798.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW89512; AAW89512; NGO0798.
GeneID3282021.
KEGGngo:NGO0798.
PATRIC20334744. VBINeiGon24812_0944.

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycNGON242231:GI2G-752-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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamPF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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_NEIG1
AccessionPrimary (citable) accession number: Q5F8H5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 15, 2005
Last modified: June 11, 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