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Q2RNG2 (GLND_RHORT) 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:Rru_A3539
OrganismRhodospirillum rubrum (strain ATCC 11170 / NCIB 8255) [Reference proteome] [HAMAP]
Taxonomic identifier269796 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesRhodospirillaceaeRhodospirillum

Protein attributes

Sequence length936 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 – 936936Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231691

Regions

Domain491 – 58595HD
Domain728 – 80982ACT 1
Domain840 – 91576ACT 2
Region1 – 372372Uridylyltransferase HAMAP-Rule MF_00277
Region373 – 727355Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q2RNG2 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 6F952FC64FC6A76C

FASTA936105,094
        10         20         30         40         50         60 
MTIPRIRQPR AVIDRKALTV VLEDLAATVT DNRERRARLL AVLKGALGDG RAEVRRRFLE 

        70         80         90        100        110        120 
EKGTGAAVFA ENSHLMDQII RLLFDFTTTH VYPRANRTIG EQMTVLAVGG YGRGEMSPQS 

       130        140        150        160        170        180 
DVDLLFLLPY KATPLHEQVV EYMLYTLWDM GLKVGHATRS IEECIRQARG DLTIRTAMLE 

       190        200        210        220        230        240 
TRYLWGDRAL YGQLKTKFWT GVVTGTGPDF VEAKLAERDE RHLRMGDSRY VLEPNIKDGK 

       250        260        270        280        290        300 
GGLRDLHTLL WIARYIYGVS DMRELVELGV LSADAATKFG RARAFLWTVR CHLHYLADRP 

       310        320        330        340        350        360 
EERLTFDVQP AIAARMGYTD RNSGRGVERF MKHYFLMAKT VGDLTRIFCA VLEDQQKRRP 

       370        380        390        400        410        420 
ILSIATLLMR KRNLGDFVLD GGRLAVAGRG AFREHPLQLI SLFKVAHDHG LDIHPDTLRL 

       430        440        450        460        470        480 
VTEHLPTVTL LRNDAKANAL FMEILTSRKD PELALRQLSE SGVLARFIPD FGRVTAQMQF 

       490        500        510        520        530        540 
DMYHVYTTDE HTIRAIGLLH RLETGALRDR MPAAADAVHK VQSRRALYLA VLLHDIAKGR 

       550        560        570        580        590        600 
GGDHSILGAE VAMRLGPRLG MSEEETETVA WLVRHHLDMS RTAFKRDLDD IKTILDFTGL 

       610        620        630        640        650        660 
VQSVERLHLL LALTTVDILA VGPAVWNNWK SSLLRELYTH SKDVLTSGFQ AEARDKRVAH 

       670        680        690        700        710        720 
KREELAAALA DWPQASRERY LDLHYPAYWL TFDSATHLRH ARMLRRARDA GLTVAVEVLP 

       730        740        750        760        770        780 
DPERAVSEVL VATDDHPGLF SKIAGAMALA GVNILDAKIT TMSDGGALDI FTVQTLEGHA 

       790        800        810        820        830        840 
IEKEERIARL AKTVRDVLTG DLPLEKALRR QPPRLPERTR HLTVPPRVIV DNQASKTHTV 

       850        860        870        880        890        900 
IEINGRDRPG FLYAVTRALT DVAVQISSAR VSTYGERVVD SFYVKDVFGM KIVHRAKLAQ 

       910        920        930 
IREALEAAIT QTVPRKVEEG AEQGAEKADA GEIVAA 

« Hide

References

[1]"Complete sequence of the chromosome of Rhodospirillum rubrum ATCC 11170."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Mavrommatis K., Richardson P., Zhang Y., Roberts G., Reslewic S., Zhou S., Schwartz D.C.
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000230 Genomic DNA. Translation: ABC24333.1.
RefSeqYP_428620.1. NC_007643.1.

3D structure databases

ProteinModelPortalQ2RNG2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269796.Rru_A3539.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC24333; ABC24333; Rru_A3539.
GeneID3836994.
KEGGrru:Rru_A3539.
PATRIC23330876. VBIRhoRub82919_3656.

Phylogenomic databases

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

Enzyme and pathway databases

BioCycRRUB269796:GCN1-3602-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]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
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_RHORT
AccessionPrimary (citable) accession number: Q2RNG2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: January 24, 2006
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