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Q8EGH8 (GLND_SHEON) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 76. 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:SO_1626
OrganismShewanella oneidensis (strain MR-1) [Reference proteome] [HAMAP]
Taxonomic identifier211586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length861 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 – 861861Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192767

Regions

Domain436 – 566131HD
Domain676 – 75681ACT 1
Domain784 – 86178ACT 2
Region1 – 317317Uridylyltransferase HAMAP-Rule MF_00277
Region318 – 675358Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q8EGH8 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 178797ACAE4EAE80

FASTA86198,320
        10         20         30         40         50         60 
MNTALLAKQS LIEQNQTLLA RFKAKTPIEE LVTQRCQFVD SLVKQAWQQH GLDQYPIALI 

        70         80         90        100        110        120 
AVGGYGRGEL HPHSDVDLLF LFEGELSKAA ETTLSEFIAF LWDANLEIGH SVRTLDDTLR 

       130        140        150        160        170        180 
LGRDDITIAT NLLEARLLTG PETLFDQLYD AIRQSDFWTS SNFFIAKRDE QTARHAKASA 

       190        200        210        220        230        240 
FDLEPNIKSC PGGLRDIQTI AWVAMRHFGA SRLEELVEYE FLEPAELEEL LECQHFLWKL 

       250        260        270        280        290        300 
RFALHMAVGR DENRLLFDVQ RQVAELMGYE DATQLAVEQM MKRYYRTVRR VMELNEMLLQ 

       310        320        330        340        350        360 
LFKRATLGHT KALEIQAIDD NYQRRGAFIE ALSDDLFDSG EEIVRLFVHI AKNSNIKGIY 

       370        380        390        400        410        420 
APTLRSLRRA RRAQLQPLQE NPLCRQAFME ILKHPRGIAA LSLMHKHGVL SAYLPAWRNI 

       430        440        450        460        470        480 
EGQMQFDLFH AYTVDEHTHR LLLNIERFSQ PEQKEEFPLG SVLINQLPKK GLLVLGAIFH 

       490        500        510        520        530        540 
DIAKGRGGDH SKLGSSDALA FCKLHGLNDH DGRLVAWLVE NHLVMSVTAQ RRDISDPDVV 

       550        560        570        580        590        600 
ADFASKVRDA VHLSYLYCLT VADICATNEK TWNNWKGSLL RDLYFSTQRV LARGKEKPVD 

       610        620        630        640        650        660 
IRARVREYQA KAKKELLRRG IKEKDLDTLW QRFKADYFLR HQPNQVAWHA EAILKHKQVD 

       670        680        690        700        710        720 
EPLVLVSKHT TRGGTELFVY CQDRPKLFAT VMAVLDNKNI NVHDANIMTS KDNYALDTFV 

       730        740        750        760        770        780 
ILEQDGEPVS QLSRIQSIRK ALEKALASDN PKLPRFRKLS RKMKPFNVPT QVSFLESNRH 

       790        800        810        820        830        840 
GTSMMELIAL DTPGLLAKVG DIFYRCNTTL LSAKITTIGE RAEDFFILQT NDGLQLNETQ 

       850        860 
EHTLKEALIS ALSAINTEST N 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014299 Genomic DNA. Translation: AAN54681.1.
RefSeqNP_717237.1. NC_004347.2.

3D structure databases

ProteinModelPortalQ8EGH8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING211586.SO_1626.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN54681; AAN54681; SO_1626.
GeneID1169421.
KEGGson:SO_1626.
PATRIC23522886. VBISheOne101494_1565.

Phylogenomic databases

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

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_SHEON
AccessionPrimary (citable) accession number: Q8EGH8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: February 19, 2014
This is version 76 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