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P27249 (GLND_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:b0167, JW0162
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length890 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modifies, by uridylylation and deuridylylation, the PII regulatory proteins GlnB and GlnK, 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. Ref.7 Ref.9 Ref.10 Ref.11

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. Ref.7 Ref.9 Ref.10 Ref.11

Cofactor

Magnesium. Mg2+ appears to be the physiologically relevant metal ion cofactor for both transferase and uridylyl-removing activities. Ref.9

Enzyme regulation

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity. Both reactions are activated by ATP and 2-ketoglutarate, via the binding of these effector molecules to the substrates PII and PII-UMP. Ref.8 Ref.9 Ref.10 Ref.11

Subunit structure

Monomer. Can also form homooligomers that are much less active. Ref.7

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. Ref.11

Miscellaneous

The transferase reaction proceeds by an ordered bi-bi kinetic mechanism, with PII binding before UTP and pyrophosphate (PPi) released before PII-UMP. The uridylyl-removing reaction proceeds with rapid equilibrium binding of substrate and random release of products (Ref.9).

Sequence similarities

Belongs to the GlnD family.

Contains 2 ACT domains.

Contains 1 HD domain.

Biophysicochemical properties

Kinetic parameters:

kcat is 137 min(-1) for the UTase reaction. kcat is 2.7 min(-1) for the UR reaction in the absence of glutamine, and 6.5 min(-1) in the presence of 2.5 mM glutamine.

KM=3.0 µM for GlnB protein Ref.9

KM=40 µM for UTP

KM=2.3 µM for uridylyl-[protein-PII] (in the absence of glutamine)

KM=0.82 µM for uridylyl-[protein-PII] (in the presence of 2.5 mM glutamine)

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 890890Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000192732

Regions

Domain468 – 601134HD
Domain709 – 78981ACT 1
Domain816 – 89075ACT 2
Region1 – 349349Uridylyltransferase HAMAP-Rule MF_00277
Region350 – 708359Uridylyl-removing HAMAP-Rule MF_00277

Experimental info

Mutagenesis931G → L or V: Loss of UTase activity, while no significant effect on UR activity. Ref.11
Mutagenesis941G → D: Loss of UTase activity, while no significant effect on UR activity. Ref.11
Mutagenesis1071D → A, V or Y: Loss of UTase activity, while no significant effect on UR activity. Ref.11
Mutagenesis514 – 5152HD → AA or QN: Loss of UR activity, while no significant effect on UTase activity.
Sequence conflict471L → S in AAA23878. Ref.1
Sequence conflict2251G → A Ref.3
Sequence conflict357 – 3582RG → TR in AAA23878. Ref.1
Sequence conflict5231D → H in AAA23878. Ref.1
Sequence conflict7031A → R in CAA79887. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P27249 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 6FF0006341A71D34

FASTA890102,390
        10         20         30         40         50         60 
MNTLPEQYAN TALPTLPGQP QNPCVWPRDE LTVGGIKAHI DTFQRWLGDA FDNGISAEQL 

        70         80         90        100        110        120 
IEARTEFIDQ LLQRLWIEAG FSQIADLALV AVGGYGRGEL HPLSDVDLLI LSRKKLPDDQ 

       130        140        150        160        170        180 
AQKVGELLTL LWDVKLEVGH SVRTLEECML EGLSDLTVAT NLIESRLLIG DVALFLELQK 

       190        200        210        220        230        240 
HIFSEGFWPS DKFYAAKVEE QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF 

       250        260        270        280        290        300 
GATSLDEMVG FGFLTSAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN 

       310        320        330        340        350        360 
YSGEGNEPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPI DDEFQLRGTL 

       370        380        390        400        410        420 
IDLRDETLFM RQPEAILRMF YTMVHNSAIT GIYSTTLRQL RHARRHLQQP LCNIPEARKL 

       430        440        450        460        470        480 
FLSILRHPGA VRRGLLPMHR HSVLGAYMPQ WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE 

       490        500        510        520        530        540 
SFASEETRQR HPLCVDVWPR LPSTELIFIA ALFHDIAKGR GGDHSILGAQ DVVHFAELHG 

       550        560        570        580        590        600 
LNSRETQLVA WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTENRLRYL VCLTVADICA 

       610        620        630        640        650        660 
TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL RMDNIDEEAL 

       670        680        690        700        710        720 
HQIWSRCRAN YFVRHSPNQL AWHARHLLQH DLSKPLVLLS PQATRGGTEI FIWSPDRPYL 

       730        740        750        760        770        780 
FAAVCAELDR RNLSVHDAQI FTTRDGMAMD TFIVLEPDGN PLSADRHEVI RFGLEQVLTQ 

       790        800        810        820        830        840 
SSWQPPQPRR QPAKLRHFTV ETEVTFLPTH TDRKSFLELI ALDQPGLLAR VGKIFADLGI 

       850        860        870        880        890 
SLHGARITTI GERVEDLFII ATADRRALNN ELQQEVHQRL TEALNPNDKG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and sequencing of gldD, the gene for uridylyl transferase and uridyl removing enzyme of E. coli."
Park S.-C., Kim I.H., Rhee S.G.
Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"The genes of the glutamine synthetase adenylylation cascade are not regulated by nitrogen in Escherichia coli."
van Heeswijk W.C., Rabenberg M., Westerhoff H.V., Kahn D.D.
Mol. Microbiol. 9:443-458(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]"Cascade control of Escherichia coli glutamine synthetase. Purification and properties of PII uridylyltransferase and uridylyl-removing enzyme."
Garcia E., Rhee S.G.
J. Biol. Chem. 258:2246-2253(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
[8]"An alternative PII protein in the regulation of glutamine synthetase in Escherichia coli."
van Heeswijk W.C., Hoving S., Molenaar D., Stegeman B., Kahn D., Westerhoff H.V.
Mol. Microbiol. 21:133-146(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
Strain: K12.
[9]"Enzymological characterization of the signal-transducing uridylyltransferase/uridylyl-removing enzyme (EC 2.7.7.59) of Escherichia coli and its interaction with the PII protein."
Jiang P., Peliska J.A., Ninfa A.J.
Biochemistry 37:12782-12794(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, KINETIC PARAMETERS, SUBSTRATE SPECIFICITY, KINETIC MECHANISM.
[10]"Characterization of the GlnK protein of Escherichia coli."
Atkinson M.R., Ninfa A.J.
Mol. Microbiol. 32:301-313(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION WITH GLNK AS SUBSTRATE, CATALYTIC ACTIVITY, ENZYME REGULATION.
[11]"Mutagenesis and functional characterization of the four domains of GlnD, a bifunctional nitrogen sensor protein."
Zhang Y., Pohlmann E.L., Serate J., Conrad M.C., Roberts G.P.
J. Bacteriol. 192:2711-2721(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, DOMAIN, ENZYME REGULATION, MUTAGENESIS OF GLY-93; GLY-94; ASP-107 AND 514-HIS-ASP-515.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96431 Genomic DNA. Translation: AAA23878.1.
Z21842 Genomic DNA. Translation: CAA79887.1.
U70214 Genomic DNA. Translation: AAB08596.1.
U00096 Genomic DNA. Translation: AAC73278.1.
AP009048 Genomic DNA. Translation: BAE76045.1.
PIRG64740.
RefSeqNP_414709.1. NC_000913.3.
YP_488469.1. NC_007779.1.

3D structure databases

ProteinModelPortalP27249.
SMRP27249. Positions 436-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9779N.
IntActP27249. 24 interactions.
MINTMINT-1252261.
STRING511145.b0167.

Proteomic databases

PaxDbP27249.
PRIDEP27249.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73278; AAC73278; b0167.
BAE76045; BAE76045; BAE76045.
GeneID12930753.
944863.
KEGGecj:Y75_p0163.
eco:b0167.
PATRIC32115441. VBIEscCol129921_0172.

Organism-specific databases

EchoBASEEB1383.
EcoGeneEG11411. glnD.

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
PhylomeDBP27249.
ProtClustDBPRK05007.

Enzyme and pathway databases

BioCycEcoCyc:GLND-MONOMER.
ECOL316407:JW0162-MONOMER.
MetaCyc:GLND-MONOMER.
BRENDA2.7.7.59. 2026.
SABIO-RKP27249.

Gene expression databases

GenevestigatorP27249.

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...

Other

PROP27249.

Entry information

Entry nameGLND_ECOLI
AccessionPrimary (citable) accession number: P27249
Secondary accession number(s): Q2MCG1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 136 of the entry and version 2 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene