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Q3BVJ6 (GLND_XANC5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:XCV1486
OrganismXanthomonas campestris pv. vesicatoria (strain 85-10) [Complete proteome] [HAMAP]
Taxonomic identifier316273 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length869 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 – 869869Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231697

Regions

Domain451 – 570120HD
Domain692 – 77483ACT 1
Domain798 – 86972ACT 2
Region1 – 332332Uridylyltransferase HAMAP-Rule MF_00277
Region333 – 691359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q3BVJ6 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 98C58AD0C52AF65A

FASTA86997,326
        10         20         30         40         50         60 
MTDTPAERPD PGVAGDADWA AQARPLLVHA DMRLCKRFDQ GEPIERLVAL RARAVDQLMR 

        70         80         90        100        110        120 
NAWMRCIPAD SGLSLHAVGG YGRGELFPRS DVDVLVLGDT AAQQQHEQAL ARLFALLWDV 

       130        140        150        160        170        180 
GLPISHAVRS PAQCTAAAAD QTVLTALIES RALVADGQAR AALATAIAPP QVWPPRDFFQ 

       190        200        210        220        230        240 
AKREELLARH QRFGDTADNL EPDIKDGPGG LRDLQTLGWM ALRAFGVKDL EALVGLGHVG 

       250        260        270        280        290        300 
FDEAAALRRE REELARLRFG LHIVANRPEE RLRFDYQKTL AERLGFADDP ESLGVEKMMQ 

       310        320        330        340        350        360 
RFYRSAALIR RISDRLLQRF EEQFDGEATP EPLGGGFSLR RGYLAADAES WPDGDVLQVF 

       370        380        390        400        410        420 
ALFAQWAAHR EVRGLHSLTA RALAEVLRDL PAYDIADATA RERFMALLRG PRAVETLNRM 

       430        440        450        460        470        480 
ARLGVLGQWI PAFASVSGRM QFDLFHVYTV DQHTLMVLRN IALFAAGRAD ERFSIAHEVW 

       490        500        510        520        530        540 
PRLRKPELLL LAGLFHDIAK GRGGDHSELG AVDARAFCLA HRLSEGDTEL VTWLVEQHLR 

       550        560        570        580        590        600 
MSVTAQKQDI SDPEVIHRFA TLVGTRERLD YLYLLTCADI AGTSPKLWNA WKDRLLADLY 

       610        620        630        640        650        660 
FAARRALREG LEHPPPREER LREARESART LMQAQGHDDV TIDRQFAGMP DENFLRFRPE 

       670        680        690        700        710        720 
QLAWQAASLI EVEIGQTLVK ARRAVPDNDA LEVFVYSPDR DGLFAAIVAT LDRKGYGIHR 

       730        740        750        760        770        780 
ARVLDAPHDA IFDVFEVLPQ ETYADGDPQR LAATLRQVLA GDLHKVRPAR RAVPRQLRHF 

       790        800        810        820        830        840 
RFAPRVEFSE SAGGRRTRIS LVAPDRPGLL ADVAHVLRMQ HLRVHDARIA TFGERAEDQF 

       850        860 
QITDEHDRPL SESARQALRD ALCACLDPV 

« Hide

References

[1]"Insights into genome plasticity and pathogenicity of the plant pathogenic Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete genome sequence."
Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., Niesbach-Kloesgen U. expand/collapse author list , Patschkowski T., Rueckert C., Rupp O., Schneiker S., Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., Kaiser O.
J. Bacteriol. 187:7254-7266(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 85-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM039952 Genomic DNA. Translation: CAJ23117.1.
RefSeqYP_363217.1. NC_007508.1.

3D structure databases

ProteinModelPortalQ3BVJ6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316273.XCV1486.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ23117; CAJ23117; XCV1486.
GeneID3729265.
KEGGxcv:XCV1486.
PATRIC24092452. VBIXanCam71633_1721.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK04374.

Enzyme and pathway databases

BioCycXCAM316273:GJF8-1526-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. 1 hit.
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_XANC5
AccessionPrimary (citable) accession number: Q3BVJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 22, 2005
Last modified: February 19, 2014
This is version 61 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