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A7N1X9 (GLND_VIBCB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. 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:VIBHAR_03239
OrganismVibrio campbellii (strain ATCC BAA-1116 / BB120) [Complete proteome] [HAMAP]
Taxonomic identifier338187 [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_1000022355

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
A7N1X9 [UniParc].

Last modified October 2, 2007. Version 1.
Checksum: C615AE9FF2E84D6E

FASTA874100,710
        10         20         30         40         50         60 
MTLQSPLTFR DEQINIGELK QELEKFSSYQ KEEFLQHHPV TNLVLSRAEY MDLLLNRLWQ 

        70         80         90        100        110        120 
HFGFKDIHNI SLVAVGGYGR GELHPLSDID ILILSNNKLP NALEAKISEF ITLLWDLRLE 

       130        140        150        160        170        180 
VGHAVRTVDE CAEIGRADLT VATNLQEARL LCGSEDTFQA LKKVVLSDSF WPSETFYRAK 

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

       250        260        270        280        290        300 
EYRELVECQD ILWRVRFALH IELRRYDNRL TFAHQAQVAE HLGYVGEGNR GVEMMMKEFY 

       310        320        330        340        350        360 
RTLRRVAELN KMLLKLFDQA IINGGASEDA EIIDEDFQRR GALIEARKPA LFQARPETIL 

       370        380        390        400        410        420 
DMFLHIANDS SIEGVSPPTL RQLRTARRRL NKFLHTIPEA REKFMALCRH PNALHKAFSL 

       430        440        450        460        470        480 
MHKLGVLAAY LPQWSQIVGQ MQFDLFHVYT VDEHSIRLLK HINTFSYAEN HSKHPICCEV 

       490        500        510        520        530        540 
YPRIQKKELL ILAAIFHDIG KGRGGDHSVI GEGEAYDFCI EHGLSKPEAK LVSWLVRHHL 

       550        560        570        580        590        600 
LMSVTAQRRD IYDPDVITEF AKQVRDEEYL EYLVCLTVAD ICATNPELWN SWKRTLLAEL 

       610        620        630        640        650        660 
FYSTQRALRR GLENPVDVRE RIRHNQQMAS AQLRKEGFSA REIEVLWQRF KADYFLRHTH 

       670        680        690        700        710        720 
KQIAWHCENL LRMEDTSKPL VLISKKATRG GTEVFVYSPD QPALFATVVA ELDRRNFNVH 

       730        740        750        760        770        780 
DAQIMTSKDG YVLDTFMVLD QHGKAIEEGR HSAVTKHITH VLEDGRPTKI KTRRTPNKLQ 

       790        800        810        820        830        840 
HFNVKTKVDF LPTKSKKRTL MEFVALDTPG LLAKVGRTFA DLGINLHAAK ITTIGERAED 

       850        860        870 
LFILTSEAGG RLSEEQQTEL REKLIEKLSD SVSA 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000789 Genomic DNA. Translation: ABU72188.1.
RefSeqYP_001446415.1. NC_009783.1.
YP_008527642.1. NC_022269.1.

3D structure databases

ProteinModelPortalA7N1X9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338187.VIBHAR_03239.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABU72188; ABU72188; VIBHAR_03239.
GeneID16817140.
5556041.
KEGGvha:VIBHAR_03239.
PATRIC20133113. VBIVibHar24526_3086.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05007.

Enzyme and pathway databases

BioCycVHAR338187:GJCH-3229-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. 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_VIBCB
AccessionPrimary (citable) accession number: A7N1X9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 2, 2007
Last modified: February 19, 2014
This is version 47 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