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B7VIS0 (GLND_VIBSL) 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:VS_2355
OrganismVibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32)) [Complete proteome] [HAMAP]
Taxonomic identifier575788 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

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_1000132531

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
B7VIS0 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: F87E5B8C89D7356D

FASTA873100,638
        10         20         30         40         50         60 
MPYQCPITFN DEQLEICELK NQLEIFTQYQ KSEFLNHHPV TDLVLLRSEY MDLLLNRLWE 

        70         80         90        100        110        120 
HFGFSKLPHI ALVAVGGYGR GELHPLSDID ILIVSQRTLP SALGEKVSQF ITLLWDLKLE 

       130        140        150        160        170        180 
VGHAVRTIAE CIEIGSDDLT VATNLQESRL LCGSEDTFQE LKLKIHSDSF WPSETFYKAK 

       190        200        210        220        230        240 
IQEQRERHAR YHDTTYNLEP DIKSTPGGLR DIHTLSWVAR RHFGATSLLE MSKYGFLTDA 

       250        260        270        280        290        300 
EYRELVECQD FLWRVRFALH IELRRYDNRL TFAHQAQVAE HLGYTGEGNR GVEMMMKEFY 

       310        320        330        340        350        360 
RTLRRVAELN KMLLKLFDQA IINGGQTQEA EILDNDFQRR GSLIEARKPA LFQARPETIL 

       370        380        390        400        410        420 
DMFIHIANDS TIEGVSPPTL RQLRTARRRL NRFLHTIPEA RDKFMDLVRH PNALHKAFSL 

       430        440        450        460        470        480 
MHKLGVLSAY LPQWSQIVGQ MQFDLFHVYT VDEHSIRLLK HINRFSQVEN HDKHPICCEV 

       490        500        510        520        530        540 
YPRVQKKELL ILAAIFHDIG KGRGGDHSEI GAVEAYSFCI EHGLSKPEAK QVAWLVQNHL 

       550        560        570        580        590        600 
LMSVTAQRRD IYDPDVITEF AKKVRDEESL ELLVCLTVAD ICATNPELWN SWKRTLLAEL 

       610        620        630        640        650        660 
FHSTQRALRR GLENPVDVRD RIRHNQQMAS ALLRKEGFSA REIEVLWQRF KADYFLRHTH 

       670        680        690        700        710        720 
TQIAWHCEHL LRLEDPSQPL VLISKKATRG GTEVFVYCKD QAALFATVVA ELDRRNFNVH 

       730        740        750        760        770        780 
DAQVMVSKDG HVLDTFIVLD QHGEAIDEAR HKAVAKHLTH VLADGRPTKI KTRRTPRNLQ 

       790        800        810        820        830        840 
HFKVKTRVEF LPTKSKKRTL MELRALDTPG LLAQVGATFA ELDINLHGAK ITTIGERAED 

       850        860        870 
LFILTSDAGG RLSEEQEQAL RERLTEHVSE LAP 

« Hide

References

[1]"Vibrio splendidus str. LGP32 complete genome."
Mazel D., Le Roux F.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LGP32.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM954972 Genomic DNA. Translation: CAV19516.1.
RefSeqYP_002417941.1. NC_011753.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING575788.VS_2355.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAV19516; CAV19516; VS_2355.
GeneID7161894.
KEGGvsp:VS_2355.
PATRIC20155290. VBIVibSpl48387_3618.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycVSPL575788:GH64-2314-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]
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_VIBSL
AccessionPrimary (citable) accession number: B7VIS0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
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