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P27249

- GLND_ECOLI

UniProt

P27249 - GLND_ECOLI

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].UniRule annotation
Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].UniRule annotation

Cofactori

Mg2+1 PublicationUniRule annotationNote: Mg(2+) appears to be the physiologically relevant metal ion cofactor for both transferase and uridylyl-removing activities.1 PublicationUniRule annotation

Enzyme regulationi

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.4 PublicationsUniRule annotation

Kineticsi

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.

  1. KM=3.0 µM for GlnB protein1 Publication
  2. KM=40 µM for UTP1 Publication
  3. KM=2.3 µM for uridylyl-[protein-PII] (in the absence of glutamine)1 Publication
  4. KM=0.82 µM for uridylyl-[protein-PII] (in the presence of 2.5 mM glutamine)1 Publication

GO - Molecular functioni

  1. [protein-PII] uridylyltransferase activity Source: EcoCyc
  2. amino acid binding Source: InterPro
  3. phosphoric diester hydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. cellular protein modification process Source: EcoCyc
  2. nitrogen compound metabolic process Source: InterPro
  3. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciEcoCyc:GLND-MONOMER.
ECOL316407:JW0162-MONOMER.
MetaCyc:GLND-MONOMER.
BRENDAi2.7.7.59. 2026.
SABIO-RKP27249.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotation
Short name:
UTase/URUniRule annotation
Alternative name(s):
Bifunctional [protein-PII] modification enzymeUniRule annotation
Bifunctional nitrogen sensor proteinUniRule annotation
Including the following 2 domains:
[Protein-PII] uridylyltransferaseUniRule annotation (EC:2.7.7.59UniRule annotation)
Short name:
PII uridylyltransferaseUniRule annotation
Short name:
UTaseUniRule annotation
[Protein-PII]-UMP uridylyl-removing enzymeUniRule annotation (EC:3.1.4.-UniRule annotation)
Short name:
URUniRule annotation
Gene namesi
Name:glnDUniRule annotation
Ordered Locus Names:b0167, JW0162
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11411. glnD.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi93 – 931G → L or V: Loss of UTase activity, while no significant effect on UR activity. 1 Publication
Mutagenesisi94 – 941G → D: Loss of UTase activity, while no significant effect on UR activity. 1 Publication
Mutagenesisi107 – 1071D → A, V or Y: Loss of UTase activity, while no significant effect on UR activity. 1 Publication
Mutagenesisi514 – 5152HD → AA or QN: Loss of UR activity, while no significant effect on UTase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 890890Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000192732Add
BLAST

Proteomic databases

PaxDbiP27249.
PRIDEiP27249.

Expressioni

Gene expression databases

GenevestigatoriP27249.

Interactioni

Subunit structurei

Monomer. Can also form homooligomers that are much less active.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
glnBP0A9Z13EBI-552032,EBI-551053
glnKP0AC553EBI-552032,EBI-559503

Protein-protein interaction databases

DIPiDIP-9779N.
IntActiP27249. 24 interactions.
MINTiMINT-1252261.
STRINGi511145.b0167.

Structurei

3D structure databases

ProteinModelPortaliP27249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini468 – 601134HDUniRule annotationAdd
BLAST
Domaini709 – 78981ACT 1UniRule annotationAdd
BLAST
Domaini816 – 89075ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 349349UridylyltransferaseAdd
BLAST
Regioni350 – 708359Uridylyl-removingAdd
BLAST

Domaini

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.1 PublicationUniRule annotation

Sequence similaritiesi

Belongs to the GlnD family.UniRule annotation
Contains 2 ACT domains.UniRule annotation
Contains 1 HD domain.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
InParanoidiP27249.
KOiK00990.
OMAiHHLLMSV.
OrthoDBiEOG6CCH44.
PhylomeDBiP27249.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006288. PII_uridyltransf. 1 hit.
SMARTiSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01693. UTase_glnD. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27249-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNTLPEQYAN TALPTLPGQP QNPCVWPRDE LTVGGIKAHI DTFQRWLGDA
60 70 80 90 100
FDNGISAEQL IEARTEFIDQ LLQRLWIEAG FSQIADLALV AVGGYGRGEL
110 120 130 140 150
HPLSDVDLLI LSRKKLPDDQ AQKVGELLTL LWDVKLEVGH SVRTLEECML
160 170 180 190 200
EGLSDLTVAT NLIESRLLIG DVALFLELQK HIFSEGFWPS DKFYAAKVEE
210 220 230 240 250
QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF GATSLDEMVG
260 270 280 290 300
FGFLTSAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN
310 320 330 340 350
YSGEGNEPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPI
360 370 380 390 400
DDEFQLRGTL IDLRDETLFM RQPEAILRMF YTMVHNSAIT GIYSTTLRQL
410 420 430 440 450
RHARRHLQQP LCNIPEARKL FLSILRHPGA VRRGLLPMHR HSVLGAYMPQ
460 470 480 490 500
WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE SFASEETRQR HPLCVDVWPR
510 520 530 540 550
LPSTELIFIA ALFHDIAKGR GGDHSILGAQ DVVHFAELHG LNSRETQLVA
560 570 580 590 600
WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTENRLRYL VCLTVADICA
610 620 630 640 650
TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL
660 670 680 690 700
RMDNIDEEAL HQIWSRCRAN YFVRHSPNQL AWHARHLLQH DLSKPLVLLS
710 720 730 740 750
PQATRGGTEI FIWSPDRPYL FAAVCAELDR RNLSVHDAQI FTTRDGMAMD
760 770 780 790 800
TFIVLEPDGN PLSADRHEVI RFGLEQVLTQ SSWQPPQPRR QPAKLRHFTV
810 820 830 840 850
ETEVTFLPTH TDRKSFLELI ALDQPGLLAR VGKIFADLGI SLHGARITTI
860 870 880 890
GERVEDLFII ATADRRALNN ELQQEVHQRL TEALNPNDKG
Length:890
Mass (Da):102,390
Last modified:June 1, 1994 - v2
Checksum:i6FF0006341A71D34
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471L → S in AAA23878. 1 PublicationCurated
Sequence conflicti225 – 2251G → A(PubMed:8202364)Curated
Sequence conflicti357 – 3582RG → TR in AAA23878. 1 PublicationCurated
Sequence conflicti523 – 5231D → H in AAA23878. 1 PublicationCurated
Sequence conflicti703 – 7031A → R in CAA79887. (PubMed:8412694)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiG64740.
RefSeqiNP_414709.1. NC_000913.3.
YP_488469.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73278; AAC73278; b0167.
BAE76045; BAE76045; BAE76045.
GeneIDi12930753.
944863.
KEGGiecj:Y75_p0163.
eco:b0167.
PATRICi32115441. VBIEscCol129921_0172.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi G64740.
RefSeqi NP_414709.1. NC_000913.3.
YP_488469.1. NC_007779.1.

3D structure databases

ProteinModelPortali P27249.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-9779N.
IntActi P27249. 24 interactions.
MINTi MINT-1252261.
STRINGi 511145.b0167.

Proteomic databases

PaxDbi P27249.
PRIDEi P27249.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC73278 ; AAC73278 ; b0167 .
BAE76045 ; BAE76045 ; BAE76045 .
GeneIDi 12930753.
944863.
KEGGi ecj:Y75_p0163.
eco:b0167.
PATRICi 32115441. VBIEscCol129921_0172.

Organism-specific databases

EchoBASEi EB1383.
EcoGenei EG11411. glnD.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
InParanoidi P27249.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.
PhylomeDBi P27249.

Enzyme and pathway databases

BioCyci EcoCyc:GLND-MONOMER.
ECOL316407:JW0162-MONOMER.
MetaCyc:GLND-MONOMER.
BRENDAi 2.7.7.59. 2026.
SABIO-RK P27249.

Miscellaneous databases

PROi P27249.

Gene expression databases

Genevestigatori P27249.

Family and domain databases

Gene3Di 1.10.3210.10. 1 hit.
HAMAPi MF_00277. PII_uridylyl_transf.
InterProi IPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF01842. ACT. 2 hits.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF006288. PII_uridyltransf. 1 hit.
SMARTi SM00471. HDc. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01693. UTase_glnD. 1 hit.
PROSITEi PS51671. ACT. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiGLND_ECOLI
AccessioniPrimary (citable) accession number: P27249
Secondary accession number(s): Q2MCG1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 1, 1994
Last modified: November 26, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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 (PubMed:9737855).1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3