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Q5QXT0 (GLND_IDILO) 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:IL0847
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length879 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 – 879879Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192738

Regions

Domain478 – 590113HD
Domain701 – 78282ACT 1
Domain809 – 87971ACT 2
Region1 – 340340Uridylyltransferase HAMAP-Rule MF_00277
Region341 – 700360Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q5QXT0 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 7DFEC2D5EA90098B

FASTA879101,332
        10         20         30         40         50         60 
MANVQEDKDF HGRWPDRTLQ PCLKDYKALL ESYQNWSAAR FVTADIDELV HHRATFFDQL 

        70         80         90        100        110        120 
ISQLWQQFQL EDEPASILAV GGYGRETLHP GSDIDLLILV GPENAEAEAK LSEKLGQFVT 

       130        140        150        160        170        180 
FLWDLHLDIG HSVRTIEDCF AQSENDITIA TNLIESRYLS GAESLYNEFH QQLLNDFPWS 

       190        200        210        220        230        240 
SRDFYQAKLD EQKQRHQQYH STSYNLEPNI KSSPGGLRDI QTVGWIAKRH FRTHSDENLV 

       250        260        270        280        290        300 
EYGYMTADEF VELRDCMNWL WRIRFALHLE AGKREDRLLF DFQPGVAVRL GYGNDGKASV 

       310        320        330        340        350        360 
ETMMKDYFKV VLRVSELNQM LLQFFHQAIL GTQDLQHAEH ISDDFAVANK LLTARHDNVF 

       370        380        390        400        410        420 
DNHCNIIRAF VCIAEHPQIQ GIHSNTIRLL RNARAQLSEP LSHDPECRDL FNQLIQHPRG 

       430        440        450        460        470        480 
CGLSFALMHH HSVLASYLSQ WQQIVGQMQF DLFHAYTVDE HTFRLVRNLY RFSDEDYQDQ 

       490        500        510        520        530        540 
FPLCEKLVAQ MDRRYCLYLA GIFHDIAKGR GGDHSELGEM DARNFCHQHG YSEEDAELVA 

       550        560        570        580        590        600 
WLVRHHLTMS VTAQKRDIHD PEVIQDFANQ VSTPERLDYL YCLTVADIRA TNQSLWNNWK 

       610        620        630        640        650        660 
ATLLEELYNA TSYLLQQDSN KPTLDIRQKI NENKASAMAL LLSAGFEKAE ILALWGRFTA 

       670        680        690        700        710        720 
DYFFRHTAEQ ISWHSQHILN LPSEQLPLIL IGDENNYGTT ELFIYHHEEG HLFASVAGVL 

       730        740        750        760        770        780 
DSQQLNILDA QILATRDGFV MDTFVVLQRD GKPLTEPHRI EEVKQQLLDV LHKRIPVPST 

       790        800        810        820        830        840 
KRPLSRRMKN FSVATEVTFI PSKHHGRTTF ELVTLDRPGL IAKLAAILQQ QNVILLAAKI 

       850        860        870 
TTIGEQAEDL FIVTTEQQTA LSDKQKKTLK AKIIKDLEF 

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References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV81687.1.
RefSeqYP_155236.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QXT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING283942.IL0847.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAV81687; AAV81687; IL0847.
GeneID3173614.
KEGGilo:IL0847.
PATRIC22139727. VBIIdiLoi21852_0849.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycILOI283942:GI0U-847-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_IDILO
AccessionPrimary (citable) accession number: Q5QXT0
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