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A6WV84 (GLND_OCHA4) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 53. 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:Oant_0157
OrganismOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168) [Complete proteome] [HAMAP]
Taxonomic identifier439375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

Protein attributes

Sequence length934 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 – 934934Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000022349

Regions

Domain496 – 613118HD
Domain737 – 81983ACT 1
Domain848 – 93184ACT 2
Region1 – 379379Uridylyltransferase HAMAP-Rule MF_00277
Region380 – 736357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A6WV84 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: E614E52BF69FF8E3

FASTA934105,778
        10         20         30         40         50         60 
MSAHDLKLEE IVNPETLRRK LNELADSTDE NYTSPTVRKV VLQALKDALV RGRANAEGML 

        70         80         90        100        110        120 
MKDGGGTLCA KRLSFLMDTL IEALFEFATT KAYPMINPSK AENMAIVAVG GYGRGGLAPG 

       130        140        150        160        170        180 
SDIDLLFLLP YKQTPWGEQV VEYMLYMLWD MGLKVGHSTR NIDECIRLSR EDMTIRTAIL 

       190        200        210        220        230        240 
DARFLTGNRE LFKTLVTRFD EEIVKDTGPE FIQAKLAERD QRHRKAGETR YLVEPNVKEG 

       250        260        270        280        290        300 
KGGQRDLHTL FWITKYFYRV KTKEELVKLG VLSRAELKLF NKAEDFLWAV RCHMHFATLK 

       310        320        330        340        350        360 
AEERLSFDIQ PEIAQRLGYT AHPGQNYVER FMKHYFLVAK DVGDLTRIIS AALEEQQAKH 

       370        380        390        400        410        420 
VPGFNRIFLT FSRRKRKLSA DGDFVSENHR INIARPEVFK EDPVNIIRLF HLADKHGLEF 

       430        440        450        460        470        480 
HPEAMQSLTR SLKLINSDLR ENPEANKLFL EILTSPRNPE LILRRMNESG VLGKFIPDFG 

       490        500        510        520        530        540 
KIVAMMQFNM YHHYTVDEHL LRCIAVLSEI EHGELENEHP LSNHLITTVK RDRNLLYVAL 

       550        560        570        580        590        600 
LLHDIAKGRP EDHSVAGARI ARRLGPRLGL TPTETETVEW LVREHLTMSM VAQSRDLNDR 

       610        620        630        640        650        660 
KTIIDFADTV QTMERLKLLL ILTVCDIKAV GPGVWNGWKG QLLRTLFYET ELVLTGGFSE 

       670        680        690        700        710        720 
LSRADRDHQA REALADRLSD WPKDKRDAYL ALHYTNYFLT VSLEDQVRHA HFIREADRNE 

       730        740        750        760        770        780 
RALATMAKPH TFEAVTEITV LAPDHPRLLS IITGACAAAG ANIVDAQIFT TGDGRALDTI 

       790        800        810        820        830        840 
LISREFDTDD DERRRAERVG KVIEDVLSGK AHLPDVLAKR TKPKRAAKAF KVEPRVEINN 

       850        860        870        880        890        900 
TLSNKFTVIE VEGLDRPGLL SELTGLISDL SLDIASAHIT TFGEKVIDSF YVTDLVGHKI 

       910        920        930 
SNATRQGNIR RKLLGVLSGE NGSKTNGRSS QAAA 

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References

[1]"Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic pathogen and symbiont of several eukaryotic hosts."
Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.
J. Bacteriol. 193:4274-4275(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49188 / DSM 6882 / NCTC 12168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000758 Genomic DNA. Translation: ABS12888.1.
RefSeqYP_001368717.1. NC_009667.1.

3D structure databases

ProteinModelPortalA6WV84.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439375.Oant_0157.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS12888; ABS12888; Oant_0157.
GeneID5379798.
KEGGoan:Oant_0157.
PATRIC20465277. VBIOchAnt73124_0167.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycOANT439375:GJIT-159-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_OCHA4
AccessionPrimary (citable) accession number: A6WV84
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: June 11, 2014
This is version 53 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