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A5UBF9 (GLND_HAEIE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 54. 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:CGSHiEE_03445
OrganismHaemophilus influenzae (strain PittEE) [Complete proteome] [HAMAP]
Taxonomic identifier374930 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length863 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 – 863863Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000022344

Regions

Domain446 – 579134HD
Domain688 – 77285ACT 1
Domain794 – 86370ACT 2
Region1 – 328328Uridylyltransferase HAMAP-Rule MF_00277
Region329 – 687359Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A5UBF9 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: FBC5A42D0FFB0B92

FASTA863100,197
        10         20         30         40         50         60 
MLFPLSLSSP LTPSAVKIER ENLKQFELEN FSRYSIFELV ENRSDFYDAL LIQLWQEMGL 

        70         80         90        100        110        120 
SEQLGISLIA VGGYGRREMF PLSDLDFLIL VEQTPIPEIE EKITQFIQFL WDCGFEVGHS 

       130        140        150        160        170        180 
VRTLQQCESE GKQDITIATN LLEARFLIGN RPHFDALNEL VKRADFWSKE GFFNAKVQEQ 

       190        200        210        220        230        240 
IERYQRYHNT AYNLEPDIKY SPGGLRDLHL LYWVALHHSG AQTLEDILQS GFIYPQEYQQ 

       250        260        270        280        290        300 
LQESRAFLFK VRFALHLILT RYDNRLLFDR QIKVSELLGF RGEGNQAVEK MMKCFFQALH 

       310        320        330        340        350        360 
RISLISNLLI QHYRENVLSS NQATVIEQLD DDFQLINQCL CLRNSLVFQE KPARILDLFF 

       370        380        390        400        410        420 
YLTQYEQANI HSDTLRQLQI SLEQLPQKLC EIPEAREKFL RLFNQPNSIK RAFMPMHQYG 

       430        440        450        460        470        480 
VLTAYLPQWQ AIEGLMQFDL FHIYTVDEHT LRVMLKLESF LSQESAQEHP IAHRIFSQLS 

       490        500        510        520        530        540 
DRTLLYIAAL FHDIAKGRGG DHAELGAKDV ANFARLHGLD RREIDTLAWL VQSHLLMSIT 

       550        560        570        580        590        600 
AQRRDIHDPE VVMNFAEAVQ NQVRLDYLTC LTVADICATN GNLWNSWKRS LFASLYEFTE 

       610        620        630        640        650        660 
QQFAQGMKEL LDYSEKSAEN RKLAQQILTQ DYSDIMPISI DQLWERCPED YFVRNTPKQI 

       670        680        690        700        710        720 
AWHTSLLVDL VEALLVKISN RFSLGGTEVF IYCQDQPHLF NKVVSTIGAK KFSIHDAQII 

       730        740        750        760        770        780 
TTQDGYVFDS FIITELNGEL VEFDRRRELE QALTLALQSE KLSALSITPN RQLQHFTVQT 

       790        800        810        820        830        840 
DVRFLHENKK EHTEMELVAL DKAGLLAQVS QIFSELNLNL LNAKITTVGE KAEDFFILTN 

       850        860 
QFGQALDSQQ REILRNVLYR NIG 

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References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittEE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000671 Genomic DNA. Translation: ABQ98110.1.
RefSeqYP_001290493.1. NC_009566.1.

3D structure databases

ProteinModelPortalA5UBF9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374930.CGSHiEE_03445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ98110; ABQ98110; CGSHiEE_03445.
GeneID5225241.
KEGGhip:CGSHiEE_03445.
PATRIC20277493. VBIHaeInf81350_0696.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycHINF374930:GJDD-668-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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamPF01842. ACT. 2 hits.
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_HAEIE
AccessionPrimary (citable) accession number: A5UBF9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: June 11, 2014
This is version 54 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