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P56884 (GLND_RHIME) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 91. 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:R00396
ORF Names:SMc01124
OrganismRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti) [Complete proteome] [HAMAP]
Taxonomic identifier266834 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

Protein attributes

Sequence length949 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 – 949949Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192760

Regions

Domain494 – 608115HD
Domain734 – 81683ACT 1
Domain845 – 92682ACT 2
Region1 – 377377Uridylyltransferase HAMAP-Rule MF_00277
Region378 – 733356Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
P56884 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: EF549C1B0D8540A0

FASTA949106,382
        10         20         30         40         50         60 
MARHETSFPE ILDVAALRAR CDFIASAHAE QREPMRRALL AAFKEANVAG RAKARELLAA 

        70         80         90        100        110        120 
DGAGIKCAER ISWLQDQLIT LLHDFVLNQV FDAAKAPEAS RIAVTAVGGY GRGTLAPGSD 

       130        140        150        160        170        180 
IDLLFLLPAK KAVWAEPAIE FMLYILWDLG FKVGHATRTI EECIRLSRAD MTIRTAILEC 

       190        200        210        220        230        240 
RYVCGSAALA NELETRFDHE IVRNTGPEFI AAKLAERDER HRKAGDTRYL VEPNVKEGKG 

       250        260        270        280        290        300 
GLRDLHTLFW ISKYFYRVKD SADLVKLGVL SKQEYKLFQK AEDFLWAVRC HMHFLTGKAE 

       310        320        330        340        350        360 
ERLSFDIQRE IAEALGYHDH PGLSAVERFM KHYFLVAKDV GDLTRIFCSA LEDQQAKDTP 

       370        380        390        400        410        420 
GITGVISRFR NRVRKIAGTL DFVDDGGRIA LAGTDVFKRD PVNLMRLFHI ADINGLEFHP 

       430        440        450        460        470        480 
AALKQVTRSL GLITPHLREN EEANRLFLSI LTSRRNPELI LRRMNEAGVL GRFIPEFGKI 

       490        500        510        520        530        540 
VSMMQFNMYH HYTVDEHLLR SVDVLSRIER GLEEEAHPLT AMLMPGIEDR EALYVAVLLH 

       550        560        570        580        590        600 
DIAKGRPEDH SVAGAKVARK LCPRFRLTPK QTEMVVWLVE EHLTMSMVAQ TRDLNDRKTI 

       610        620        630        640        650        660 
VDFAERVQSL ERLKMLLILT VCDIRAVGPG VWNGWKGQLL RTLYYETELL LSGGFSELSR 

       670        680        690        700        710        720 
KERAKHAAHM LEEALADWPK KERQAYVRLH YQPYLLTVAL EEQVRHAGFI READRAGRTL 

       730        740        750        760        770        780 
ATMVRTHDFH AITEITVLSP DHPRLLTVIA GACAAAGANI VGAQIHTTSD GRALDTILVN 

       790        800        810        820        830        840 
REFSVAEDET RRAASIGKLI EDVLSGRKRL PEVIASRTRV KKRSRAFTVT PEVTISNTLS 

       850        860        870        880        890        900 
NKFTVIEVEG LDRTGLLSEV TAVLSDLSLD IASAHITTFG EKVIDTFYVT DLVGSKITSE 

       910        920        930        940 
NRQMNIAARL KAVLAGEVDE ARERMPSGII APTPVSRVPH GSKTTKAET 

« Hide

References

« Hide 'large scale' references
[1]"glnD and mviN are genes of an essential operon in Sinorhizobium meliloti."
Rudnick P.A., Arcondeguy T., Kennedy C.K., Kahn D.
J. Bacteriol. 183:2682-2685(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021."
Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D. expand/collapse author list , Pohl T., Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C., Thebault P., Vandenbol M., Weidner S., Galibert F.
Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.
[3]"The composite genome of the legume symbiont Sinorhizobium meliloti."
Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F., Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G., Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P., Cowie A. expand/collapse author list , Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S., Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I., Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S., Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C., Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R., Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H., Wong K., Yeh K.-C., Batut J.
Science 293:668-672(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1021.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF227730 Genomic DNA. Translation: AAF37852.1.
AL591688 Genomic DNA. Translation: CAC41833.1.
RefSeqNP_384502.1. NC_003047.1.

3D structure databases

ProteinModelPortalP56884.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266834.SMc01124.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC41833; CAC41833; SMc01124.
GeneID1232030.
KEGGsme:SMc01124.
PATRIC23629999. VBISinMel96828_1769.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261779.
KOK00990.
OMAHHLLMSV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycSMEL266834:GJF6-407-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_RHIME
AccessionPrimary (citable) accession number: P56884
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: June 11, 2014
This is version 91 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