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Q5NZH8 (GLND_AROAE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 70. 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:AZOSEA34110
ORF Names:ebA5982
OrganismAromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaRhodocyclalesRhodocyclaceaeAromatoleum

Protein attributes

Sequence length862 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 – 862862Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192715

Regions

Domain448 – 553106HD
Domain686 – 76580ACT 1
Domain794 – 86269ACT 2
Region1 – 328328Uridylyltransferase HAMAP-Rule MF_00277
Region329 – 685357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q5NZH8 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: FA31DCA7E434257E

FASTA86298,195
        10         20         30         40         50         60 
MSTAAIPTDA AVQAAIAEAR ARLADGSMRI RMAYEGHPAT STVLKGRAHL VDETIHRLWR 

        70         80         90        100        110        120 
ACAMPADVAL LAVGGYGRGE LFPCSDVDLM VLLPDTADDA MQARLSVLLG ALWDVGLEIG 

       130        140        150        160        170        180 
HSARTVAEAI DAAEQDITVQ TNLLESRLLE GNRPLFEEFC RRYRALLDVR VFFKAKQLEQ 

       190        200        210        220        230        240 
EKRYARYNDT PYALEPNCKE SPGGLRDLQM LGWIARAAGL GRNWRDLARR RLITGAEARD 

       250        260        270        280        290        300 
LRSIERFLQH VRIRLHYLTG RSEDRLLFDY QERLASALGI EATAAKRASE VFMQRYYVNA 

       310        320        330        340        350        360 
KKVTQTNTIL LQNYGVEIFP RRAGAAIVIN ERFQAVRELL DMREDDTFAR HPSALLECFL 

       370        380        390        400        410        420 
ILQQRSELKG MTARTLRALW LNRKRINAAF RADPHNRELF VAILQQKRGI VHEFRRMNQY 

       430        440        450        460        470        480 
GILSGYLPSW RRIVGQMQHD LFHVYTVDQH IMMVLRNMRR FTMGEHAHEY PLMAQLIMAF 

       490        500        510        520        530        540 
DRHWLLYVAA LFHDIAKGRG GDHSKLGTID AREFCEHHHL AREDADLVVW LVEHHLTMSH 

       550        560        570        580        590        600 
VAQKEDTSDP AVIGRFADTV GTERRLTALY LLTHADIRGT SPKVWNGWKG KLLEDLFFAT 

       610        620        630        640        650        660 
RRLLRGATPQ EALGLDDRQE NARALLRYHG LRPGVEDALW AQLDAVYFMR HSAEEIAWHS 

       670        680        690        700        710        720 
RTLYYRPDAL EPVVKARVSD ADQGVQVMVF TRDQKDLFVR LTGFFGRLGF SILDAKVHTT 

       730        740        750        760        770        780 
RHGYALDSFM LQDPGNAEHY RDVITLIEHE LTERLKKSAP PDRPSAGRLS RQVKHFPITP 

       790        800        810        820        830        840 
RVSILPDESG RHYILSLTAA DRRGLLFAVA EVLAQNGIVL HTAKIATLGE RVEDTFLLSG 

       850        860 
NGLSQDARVV KIERELLQRL HI 

« Hide

References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: EbN1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR555306 Genomic DNA. Translation: CAI09536.1.
RefSeqYP_160437.1. NC_006513.1.

3D structure databases

ProteinModelPortalQ5NZH8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING76114.ebA5982.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI09536; CAI09536; ebA5982.
GeneID3179129.
KEGGeba:ebA5982.
PATRIC20973043. VBIAroAro98752_3439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycAARO76114:GJTA-3463-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_AROAE
AccessionPrimary (citable) accession number: Q5NZH8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 4, 2005
Last modified: June 11, 2014
This is version 70 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