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Q87MD6 (GLND_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. 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:VP2320
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length874 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 – 874874Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192773

Regions

Domain452 – 584133HD
Domain693 – 77785ACT 1
Domain800 – 87475ACT 2
Region1 – 332332Uridylyltransferase HAMAP-Rule MF_00277
Region333 – 692360Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q87MD6 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 1B849BC63393E97E

FASTA874100,247
        10         20         30         40         50         60 
MPLQSPLTFS DEQINIGELK QELEKFSSTQ KQEFLNHHPV TSLVLARAEY MDLLLTRLWQ 

        70         80         90        100        110        120 
YFGFNDIYNI SLVAVGGYGR GELHPLSDID ILVLSNNKLP TALEAKISEF ITLLWDLKLE 

       130        140        150        160        170        180 
VGHAVRTVNE CAQIGRDDLT VATNLQEARL LCGSEDTFQA LKKVVLSDSF WPSETFYRAK 

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

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

       310        320        330        340        350        360 
RTLRRVAELN KMLLKLFDQA IINGGATENA EILDADFQRR GSLIEARKPA LFQARPETIL 

       370        380        390        400        410        420 
DMFLHIANDS TIEGVSPPTL RQLRTARRRL NKFLHTIPAA REKFLALCRH PNALHKAFSL 

       430        440        450        460        470        480 
MHRLGVMAAY LPQWSQIVGQ MQFDLFHAYT VDEHSIRLLK HINTFNNPDN HAKHPICCDI 

       490        500        510        520        530        540 
YPRMQKKELL IIAAIFHDIG KGRGGDHSVI GEGEAYDFCI EHGLSKPEAK LVGWLVRHHL 

       550        560        570        580        590        600 
LMSVTAQRRD IYDPDVITEF AKQVRDEESL EYLVCLTVAD ICATNPELWN AWKRTLLAEL 

       610        620        630        640        650        660 
FYSTQRALRR GLENPVDVRE RIRHNQQMAS ALLRKEGFSA RQIEVLWQRF KADYFLRHTH 

       670        680        690        700        710        720 
TQIAWHCAHL LRMDDPNKPL VLISKKATRG GTEVFVYTKD QPALFATVVA ELDRRNFNVH 

       730        740        750        760        770        780 
DAQIMTSKDG HVIDTFMVLD QHGEAIDESR HAAVIKHLTH VLEAGRPTKI KTRRTPNKLQ 

       790        800        810        820        830        840 
HFNVKTKVDF LPTKGKKHTL MEFVALDTPG LLAKVGRTFA DLNINLHGAK ITTIGERAED 

       850        860        870 
LFILTSEAGG RLSEEQQNEL RDKLIEKLSD AVTA 

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References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC60583.1.
RefSeqNP_798699.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87MD6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP2320.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC60583; BAC60583; BAC60583.
GeneID1189833.
KEGGvpa:VP2320.
PATRIC20142786. VBIVibPar50997_2222.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-2377-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_VIBPA
AccessionPrimary (citable) accession number: Q87MD6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2003
Last sequence update: June 1, 2003
Last modified: June 11, 2014
This is version 76 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