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Q2N784 (GLND_ERYLH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 58. 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:ELI_11825
OrganismErythrobacter litoralis (strain HTCC2594) [Complete proteome] [HAMAP]
Taxonomic identifier314225 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesErythrobacteraceaeErythrobacter

Protein attributes

Sequence length919 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 – 919919Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000022343

Regions

Domain490 – 592103HD
Domain728 – 81184ACT 1
Domain839 – 91981ACT 2
Region1 – 373373Uridylyltransferase HAMAP-Rule MF_00277
Region374 – 727354Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q2N784 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: B532D60CE3188D12

FASTA919104,003
        10         20         30         40         50         60 
MTDPKVPRQR RIIDRRKLAA AVEALAEQQG EKARPAVLKV LREALEKGRD ELSQRLLDRP 

        70         80         90        100        110        120 
SAGHQITAGH AFLVDQLVRV IFDHVTTHLY PVANRSSSER IAVLAVGGYG RAEMAPQSDV 

       130        140        150        160        170        180 
DIAFLHPSRR TPWCEQVTEA MLYFLWDLGF KVGQSSRTPE DMVRMAREDL TIRTALLEAR 

       190        200        210        220        230        240 
FVWGDRELYD EARKRFWSEV VNGTERQFVA EKLAERDARH ERMGGTRYVV EPNVKEGKGG 

       250        260        270        280        290        300 
LRDLQTLYWI GKYIHRARGA AELVDAGLLT ETEYHGFRRA EGFLLAVRCH LHEITGRPED 

       310        320        330        340        350        360 
RLTFDFQKQI AERMRFAERR EKSAVERFMQ YYFLQVKRVG SLTGVFLAQM DQQFARKRAR 

       370        380        390        400        410        420 
TGLLAGFNAK SRMLKGYTVF GGKIAAPGDN WFRDDPVRLI EIFQLAEANG LEIDPRSMRQ 

       430        440        450        460        470        480 
ADRDSVLIKD QVRNDPRANA IFLDLLCGRN DPETALRWMN EAGVFGKFVP DFGRVNAQMQ 

       490        500        510        520        530        540 
FNMYHHYTVD EHTIRAIGFL SKIEKGELAK EHPRSTREIH KVKSRRVAFV AALLHDIAKG 

       550        560        570        580        590        600 
RGGDHSILGA EVAEELCPRF GLDEDETDLV AWLVLQHLLM SSTAQKRDLT DPKTIEDFVA 

       610        620        630        640        650        660 
EVQSLERLRH LAILTSVDIR AVGPGTWNSW KGQLLGELYD AAHERLRLGH MKHHRSERVA 

       670        680        690        700        710        720 
AKKEAVREAL GGKAALLEKH GRLLPDSYWI AEPENVISRN IVQYDVAREI SEDLSIHCEF 

       730        740        750        760        770        780 
DEERGATLVT VIAADHPGLF YRIAGGIHLA GGNIIDARIH TTRNGWAIDN YLVQDPVGQP 

       790        800        810        820        830        840 
FAEERQLARI EQAIADAIAN RGELVPKLAK RPLKQTRAGA FDVRPRVLFD NDASGRFTVI 

       850        860        870        880        890        900 
EVNARDRAAL LNRLGRALFE NQVIVQSAHI TAYGERAADT FYVTDLTGAK ITDESRMDTI 

       910 
RQALLDAASD ARQAELEPA 

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References

[1]"Complete genome sequence of Erythrobacter litoralis HTCC2594."
Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.
J. Bacteriol. 191:2419-2420(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HTCC2594.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000157 Genomic DNA. Translation: ABC64457.1.
RefSeqYP_459254.1. NC_007722.1.

3D structure databases

ProteinModelPortalQ2N784.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314225.ELI_11825.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC64457; ABC64457; ELI_11825.
GeneID3871505.
KEGGeli:ELI_11825.
PATRIC21861869. VBIEryLit102657_2349.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycELIT314225:GHLE-2407-MONOMER.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR005105. GlnD_Uridyltrans_N.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamPF03445. DUF294. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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_ERYLH
AccessionPrimary (citable) accession number: Q2N784
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 7, 2006
Last modified: June 11, 2014
This is version 58 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