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O69873 (GLND_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 98. 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:SCO5585
ORF Names:SC2E1.02
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length835 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 – 835835Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192770

Regions

Domain432 – 549118HD
Domain651 – 73686ACT 1
Domain765 – 83571ACT 2
Region1 – 316316Uridylyltransferase HAMAP-Rule MF_00277
Region317 – 650334Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
O69873 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 551296D8BE77DE5D

FASTA83589,047
        10         20         30         40         50         60 
MTDEAEDSGP GGYAAARLRL LTEGARSGPP RRRALAELTD GWLAGLFGAA TEEHTGISLV 

        70         80         90        100        110        120 
AVGGYGRGEL SPRSDLDLLL LHDGRDDKAV AALADRLWYP VWDLGIDLDH SVRTPQQARK 

       130        140        150        160        170        180 
TAGQDLKVHL GLLDARHLAG DLGLTASLRT AVLADWRNQA PKRLPELRDL CAERAERQGE 

       190        200        210        220        230        240 
LQFLLEPDLK EARGGLRDAT ALRAVAASWL ADAPREGLAE ARRRLLDVRD ALHLATGRAT 

       250        260        270        280        290        300 
DRLALQEQDQ VAAELGLLDA DALLRQVYEA ARVISYAGDV TWREVGRVLR SRSVRPRLRA 

       310        320        330        340        350        360 
MMNGRNGGKP VAERSPLAEG VVEQDGEAVL ARTARPERDP ALPLRAAAAA AQAGLPLSRH 

       370        380        390        400        410        420 
AVRRLAATAR PLPTPWPAEA REQLVTLLGS GRPTVQVWEA LEAEGLVTRL LPDWERVRCR 

       430        440        450        460        470        480 
PQRNAVHLWT VDRHLIETAV RAAGFTRRVH RPDLLLIAAL LHDIGKGWPG DHSVAGETIA 

       490        500        510        520        530        540 
RDVAARIGFD GADTAVLATL VRHHLLLVET ATRRDLDDPA TVRAVAQAVG TEHTLELLHA 

       550        560        570        580        590        600 
LTEADALATG PAAWSSWRGS LVADLVKRVS GVLAGEPQPE AESAAPTAEQ ERLAVEAFRT 

       610        620        630        640        650        660 
GGPVLALRAQ TEPPADSAPA PSSPSSPSFP SPLSSPSSPS SADGPEPLGV ELLIAVPDQA 

       670        680        690        700        710        720 
GVLPAVAGVL AMHRLTVRTA ELRSVPLPDG VEGSVLLLDW RVAAQYGSLP QAARLRADLV 

       730        740        750        760        770        780 
RALDGTLDIA ARLAERDAAH PRRRGVEPPP PRVTVAPAAS RLATVIEVRA QDAPGLLFRL 

       790        800        810        820        830 
GRALEAAGVR VRSAHVSTLG ANAVDAFYVT RGEGTPLPGD EAASVARGLE ESLRT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939124 Genomic DNA. Translation: CAA19377.1.
PIRT34770.
RefSeqNP_629719.1. NC_003888.3.

3D structure databases

ProteinModelPortalO69873.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO5585.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA19377; CAA19377; CAA19377.
GeneID1101026.
KEGGsco:SCO5585.
PATRIC23741050. VBIStrCoe124346_5676.

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000021840.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.
PhylomeDBO69873.

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_STRCO
AccessionPrimary (citable) accession number: O69873
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: May 14, 2014
This is version 98 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