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Q5H1D3 (GLND_XANOR) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 64. 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:XOO1984
OrganismXanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) [Complete proteome] [HAMAP]
Taxonomic identifier291331 [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 caution

The sequence AAW75238.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 869869Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192779

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
Q5H1D3 [UniParc].

Last modified November 8, 2005. Version 2.
Checksum: EF45D7310C81BC66

FASTA86997,350
        10         20         30         40         50         60 
MTDAPAERPD PSVAGDADWA AQARPLLVHA DMRLRKRFDQ GEPIERLVAL RARAVDQLMR 

        70         80         90        100        110        120 
NAWTRCIPAD SGLSLHAVGG YGRGELFPRS DVDVLVLGDS VAQQRHEQHL SRLFALLWDV 

       130        140        150        160        170        180 
GLPISHAVRS PTQCMVAAAD QTVLTALIES RALVADAAAR AALAAAIAPQ RVWPPRDFFQ 

       190        200        210        220        230        240 
AKREELLARH QRFGDTADNL EPDIKDGPGG LRDLQTLGCM ALRAFGVKDV EALVGLGHVG 

       250        260        270        280        290        300 
CDEAAALRRE REELARLRFG LHIVANRPEE RLRFDYQKTL AERLGFADDL ESLGVEKMMQ 

       310        320        330        340        350        360 
RFYRSAALIR RISDRLLQRF EEQFDGEATP ESLGGGFSLR RGYLAADSDS WPGDDVLQVF 

       370        380        390        400        410        420 
ALFVHWAAHR EVRGLHSLTA RALAEVLREF PAYDVADATA RELFMALLRG TRAVETLNRM 

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

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

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

       610        620        630        640        650        660 
FAARRALREG VEHPPPREER LREARESARA LMQAQGHDDA TIDRQFAGMP DENFLRFRPE 

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

       730        740        750        760        770        780 
ARVLDAPHDA IFDVFEVLPR DTYADGDPQR LAATLRQVLA GDLQQVRPAR RAVPGQLRHF 

       790        800        810        820        830        840 
RFAPRVEFSE SADGRRTRIS LVAPDRPGLL ADVAHVLRVQ HLRVHDARIA TFGERAEDQF 

       850        860 
QITDEHDRPL SESARQALRD ALCACLDPV 

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References

[1]"The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice."
Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., Go S.-J.
Nucleic Acids Res. 33:577-586(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KACC10331 / KXO85.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013598 Genomic DNA. Translation: AAW75238.1. Different initiation.
RefSeqYP_200623.1. NC_006834.1.

3D structure databases

ProteinModelPortalQ5H1D3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING291331.XOO1984.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW75238; AAW75238; XOO1984.
GeneID3264479.
KEGGxoo:XOO1984.
PATRIC24103115. VBIXanOry111333_2194.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycXORY291331:GJBV-1848-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. 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_XANOR
AccessionPrimary (citable) accession number: Q5H1D3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: June 11, 2014
This is version 64 of the entry and version 2 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