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B5F9X8 (GLND_VIBFM) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 44. 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:VFMJ11_2098
OrganismVibrio fischeri (strain MJ11) [Complete proteome] [HAMAP]
Taxonomic identifier388396 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeAliivibrio

Protein attributes

Sequence length873 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 – 873873Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000114768

Regions

Domain451 – 584134HD
Domain693 – 77785ACT 1
Domain800 – 87374ACT 2
Region1 – 332332Uridylyltransferase HAMAP-Rule MF_00277
Region333 – 692360Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
B5F9X8 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: BD26292DA8B5F8CD

FASTA873100,653
        10         20         30         40         50         60 
MKYLSPLSLS DTQLNITELK QQLTLFSQYQ INAFHQHKAV SDLVFERSHY FDQLLSRLWQ 

        70         80         90        100        110        120 
FFKFDDIANT SLIAVGGYGR SELHPLSDID ILILTENNTN DTFCQKVGEL VTLLWDLKLE 

       130        140        150        160        170        180 
IGHSVRSIAE CIEIGQNDLT VATNLQEARY ICGNKELSHQ LKLKIHSDSF WPSESFYQAK 

       190        200        210        220        230        240 
IDEQKKRHSR YHDTTYNLEP DIKSSPGGLR DIHTLSWIAR RHFGATSLLE MSQAGFLTDA 

       250        260        270        280        290        300 
EYRELLECQE FLWRVRFALH IELKRYDNRL TFGHQASVAE HLGFIGEGNR GVERMMKEFY 

       310        320        330        340        350        360 
RTLRRVAELN SMLLKIFDQA ILHQGEQDDA IIIDDDFQRR GRLIEARKPA LFQARPDTIL 

       370        380        390        400        410        420 
DMFLLMANDS TIDGVAPPTM RQLRTARRRL NRFLCEIPEA KEKFLQLTQH PNALNNAFSS 

       430        440        450        460        470        480 
MHKLGVLSAY LPQWSHIVGQ MQFDLFHAYT VDEHSIRLLK HINKFSDTTN RDKHPICCEI 

       490        500        510        520        530        540 
FPKIMKKELL IIAAIFHDIA KGRGGDHSEL GAVDAYDFCI SHGLSKPEAN LVSWLVKSHL 

       550        560        570        580        590        600 
LMSVTAQRRD IYDPDVITEF AKQVRDEERL DYLVCLTVAD ICATNPDLWN SWKRSLIADL 

       610        620        630        640        650        660 
YNATQRALRR GLENPPDLRD RIRHNQQMAS AQLRSEGFTQ WEVDALWRRF KADYFLRHTH 

       670        680        690        700        710        720 
KQIAWHASHL LRHQDKEKSL ILISKNASRG GTEIFVYSKD QPHLFATVAA ELDRRSITIY 

       730        740        750        760        770        780 
DAQVMSSKDG YALDTFMVLD QNDDPIDEER QQRLIDQLYD VKLNDQATHI KTRRPPRQLQ 

       790        800        810        820        830        840 
HFNVKTRMEF LPTKTGKRTL MEFVALDTPG LLATVGATFA QLGINLHAAK ITTIGERAED 

       850        860        870 
LFILTSDVGG RLDDDKQAEL EIALVKNVAR LSS 

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References

[1]"Complete sequence of Vibrio fischeri strain MJ11."
Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MJ11.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001139 Genomic DNA. Translation: ACH66318.1.
RefSeqYP_002156792.1. NC_011184.1.

3D structure databases

ProteinModelPortalB5F9X8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING388396.VFMJ11_2098.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH66318; ACH66318; VFMJ11_2098.
GeneID6806687.
KEGGvfm:VFMJ11_2098.
PATRIC20122660. VBIVibFis37164_2020.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

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]
PfamPF01842. ACT. 2 hits.
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_VIBFM
AccessionPrimary (citable) accession number: B5F9X8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: June 11, 2014
This is version 44 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