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Q8UIF1 (GLND_AGRT5) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 80. 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:Atu0346
ORF Names:AGR_C_606
OrganismAgrobacterium tumefaciens (strain C58 / ATCC 33970) [Reference proteome] [HAMAP]
Taxonomic identifier176299 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

Protein attributes

Sequence length942 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 – 942942Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192714

Regions

Domain523 – 60684HD
Domain730 – 81182ACT 1
Domain841 – 92080ACT 2
Region1 – 373373Uridylyltransferase HAMAP-Rule MF_00277
Region374 – 729356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q8UIF1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: B0EBDF337C7CE945

FASTA942106,204
        10         20         30         40         50         60 
MAIKDLDFSD ILDVSALKRD CDVIFKEDSK RIADIKSDLL PIFRRASTEG REKARELLKA 

        70         80         90        100        110        120 
DGSGIDCARR ISWLQDRLIE TLYDLACQHV YPKDAPQIAV AAVGGYGRGT LAPGSDIDLL 

       130        140        150        160        170        180 
FLLPAKNTPD MHKAVEFVLY LLWDLGFKVG HATRTVDECI RLSKSDMTIR TAILEVRAIC 

       190        200        210        220        230        240 
GRKSLTDDLE KRFESEVVTG TGPEFIAAKL AERDQRHRKA GDTRYLVEPN VKEGKGGLRD 

       250        260        270        280        290        300 
LHTLFWIAKY YYHVRDTADL VKLGVLSRSE LKLFEKADDF LWAVRCQMHF ITGKAEERLS 

       310        320        330        340        350        360 
FDIQREIADA LNYQPRPGLS AVERFMKHYF LVAKDVGDLT RIVCAALEDR QAKDVPGLSG 

       370        380        390        400        410        420 
VLSRFAHRVR KIPGSVEFVE DRGRIALARP DVFKNDPVNL IRLFHIADIN NLELHPDALR 

       430        440        450        460        470        480 
VVTRSLSLIN DELRENEEAN RLFLSILTSR RDPALTLRRM NEAGVLGKFI PEFGKIVAMM 

       490        500        510        520        530        540 
QFNMYHHYTV DEHLIRSVGV LSEVDKGTAV DAHPLANQLM PGVEEREALY VAVLLHDVAK 

       550        560        570        580        590        600 
GRQEDHSIAG ARVARKLCQR FRLTGKQTET VVWLIEQHLL MSMVAQTRDL HDRKTITDFA 

       610        620        630        640        650        660 
DKVQSMERLK MLLILTVCDI RAVGPGVWNG WKGQLLRSLY YETELLLSGG FSEVSRKERA 

       670        680        690        700        710        720 
QIARQALYDA LEDWGQKARR KYTKLHYEPY LLTVALEDQV RHTRFMREAD KQEKALSTMV 

       730        740        750        760        770        780 
RTHSFHAITE ITVLAPDHPR LLSIITGACA AAGANIADAQ IFTTSDGRAL DTILINREFP 

       790        800        810        820        830        840 
IDEDETRRGA NVGKLIEEVL SGKQRLPEMI ATRTKSRRKK SAFTIPPSVT ISNGLSNKFT 

       850        860        870        880        890        900 
VIEVECLDRP GLLADMTAVI ADLSLDIHSA RITTFGEKVI DTFYVTDLFG QKVTNDNRQA 

       910        920        930        940 
SIAQRLKAVM SEQEDELRDR MPNGIIAHPD VAALPAARTA KA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007869 Genomic DNA. Translation: AAK86163.2.
PIRAB2619.
B97401.
RefSeqNP_353378.2. NC_003062.2.

3D structure databases

ProteinModelPortalQ8UIF1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176299.Atu0346.

Proteomic databases

PRIDEQ8UIF1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK86163; AAK86163; Atu0346.
GeneID1132384.
KEGGatu:Atu0346.
PATRIC20810375. VBIAgrTum91616_0337.

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycAGRO:ATU0346-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. 2 hits.
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_AGRT5
AccessionPrimary (citable) accession number: Q8UIF1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: June 1, 2002
Last modified: June 11, 2014
This is version 80 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