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Q3J5H6 (GLND_RHOS4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:RHOS4_03900
ORF Names:RSP_1811
OrganismRhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158) [Reference proteome] [HAMAP]
Taxonomic identifier272943 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

Protein attributes

Sequence length930 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 fixation 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 – 930930Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231690

Regions

Domain505 – 624120HD
Domain742 – 81877ACT 1
Domain852 – 92776ACT 2
Region1 – 387387Uridylyltransferase HAMAP-Rule MF_00277
Region388 – 741354Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q3J5H6 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: F2C8D050AD54C166

FASTA930105,347
        10         20         30         40         50         60 
MAPASEAGPA QDPLFSGLIL PRSRILDAEA LTRSILAEID AAGPLDPKSA RAIAVRQMTE 

        70         80         90        100        110        120 
AKAAGNRALS ETFEARPREA RGLIRAQAAL TDGLVTAALR VACERLHPLA NPTEAERIAV 

       130        140        150        160        170        180 
LAVGGYGRAE MAPHSDVDLL FLTPWKITPW AEMVIESMLY MLWDLRLKVG HSSRTVKDCL 

       190        200        210        220        230        240 
RLGREDITIR TALLEHRFLA GHAPLAAELD ETLWNDLFRG TGAEFIDAKL EERGQRHKRQ 

       250        260        270        280        290        300 
GGQRYVLEPN VKEGKGGLRD LQTLYWIGKY LNRVPSPSGL VAAGLLTRDE FETFERAESF 

       310        320        330        340        350        360 
LWAVRCHLHY ATGRATDQLT FDLQVEVAAR MGYADTRGRR GVEVFMQDYF RHATRVGELT 

       370        380        390        400        410        420 
RVFLAQLEAR HEKREPKIMG LFRRKKRLKP EYSLVNGRID VLDPKAFLAD KLNLLRIFEE 

       430        440        450        460        470        480 
ALRTGFLIHP GAMRLIAANL HLIDEEMQHD REANRIFLDM LLRHGNPERA LRRMNELGVL 

       490        500        510        520        530        540 
GAFIPEFERI VAMMQFNVYH HYTVDEHTIQ CISTLAQIER HELDEELPIA NRILTDGISR 

       550        560        570        580        590        600 
RVIYVALLLH DIGKGRPEDH SILGAQIARR VAPRFGLTAE ECETVEWLVR YHLLMSDMAQ 

       610        620        630        640        650        660 
KRDIGDPRTV RDFAKAVRSK KRLDLLTVLT VCDIRGVGPG TWNNWKAQLL RKLYRDTVTA 

       670        680        690        700        710        720 
LDAGLESLNR ENRADEAKRA LRELLEEWDP KDLRAELARH YPPYWQALSN ATHAVFARML 

       730        740        750        760        770        780 
RGLGETEIRI DLDPDPDRDA TRACFALADH PGIFSRLAGA LALVGANVVD ARTYTTKDGY 

       790        800        810        820        830        840 
ATAVFWIQDS EGSPYEISRL PRLTSMIDKT LKGEVVAREA LKDRDKLKKR EAQFRFPTHI 

       850        860        870        880        890        900 
AFDNEGSDIY TIIEVDTRDR PGLLYDLTRT LAANNIYIAS AVIATYGAQV VDSFYVKDMF 

       910        920        930 
GLKLHQKNRQ ETLEKKLRQA IVEGAERAKQ 

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References

[1]"Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C., Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000143 Genomic DNA. Translation: ABA77958.1.
RefSeqYP_351859.1. NC_007493.2.

3D structure databases

ProteinModelPortalQ3J5H6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272943.RSP_1811.

Proteomic databases

PRIDEQ3J5H6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA77958; ABA77958; RSP_1811.
GeneID3719057.
KEGGrsp:RSP_1811.
PATRIC23150588. VBIRhoSph57909_0694.

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK05092.

Enzyme and pathway databases

BioCycRSPH272943:GJAS-403-MONOMER.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR005190. GlnE_rpt_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF03710. GlnE. 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_RHOS4
AccessionPrimary (citable) accession number: Q3J5H6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: November 8, 2005
Last modified: February 19, 2014
This is version 61 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