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Q0TLG6

- GLND_ECOL5

UniProt

Q0TLG6 - GLND_ECOL5

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, ECP_0175
Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

Functioni

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 assimilation and metabolism By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Magnesium By similarity.UniRule annotation

Enzyme regulationi

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity.UniRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. nitrogen compound metabolic process Source: InterPro
  2. regulation of nitrogen utilization Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciECOL362663:GIY5-173-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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:
[Protein-PII] uridylyltransferase (EC:2.7.7.59)
Short name:
PII uridylyltransferase
Short name:
UTase
[Protein-PII]-UMP uridylyl-removing enzyme (EC:3.1.4.-)
Short name:
UR
Gene namesi
Name:glnD
Ordered Locus Names:ECP_0175
OrganismiEscherichia coli O6:K15:H31 (strain 536 / UPEC)
Taxonomic identifieri362663 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000009182: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 890890Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000022340Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi362663.ECP_0175.

Structurei

3D structure databases

ProteinModelPortaliQ0TLG6.
SMRiQ0TLG6. Positions 469-599.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini468 – 601134HDAdd
BLAST
Domaini709 – 78981ACT 1Add
BLAST
Domaini816 – 89075ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 349349UridylyltransferaseUniRule annotationAdd
BLAST
Regioni350 – 708359Uridylyl-removingUniRule annotationAdd
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 By similarity.UniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2844.
HOGENOMiHOG000261778.
KOiK00990.
OMAiHHLLMSV.
OrthoDBiEOG6CCH44.

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.

Q0TLG6-1 [UniParc]FASTAAdd to Basket

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MNTLPEQYAN TALPTLHGQP QNPCAWPRDE LTVGGIKAHI DTFQRWLGDA    50
FDNGISAEQL IEARTEFIDQ LLQRLWIEAG FSQIADLALV AVGGYGRGEL 100
HPLSDIDLLI LSRKKLPDDQ AQKVGELLTL LWDVKLEVGH SVRTLEECML 150
EGLSDLTVAT NLIESRLLIG DVALFLELQK HIFSEGFWPS DKFYAAKVEE 200
QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF GATSLDEMVG 250
FGFLTSAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN 300
YSGEGNEPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPI 350
DDEFQLRGTL IDLRDETLFM RQPEAILRMF YTMVRNSAIT GIYSTTLRQL 400
RHARRHLQQP LCNIPEARKL FLSILRHPGA VRRGLLPMHR HSVLGAYMPQ 450
WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE SFASEETRQR HPLCVDVWPR 500
LPSTELIFIA ALFHDIAKGR GGDHSILGAQ DVVHFAELHG LNSRETQLVA 550
WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTENRLRYL VCLTVADICA 600
TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL 650
RMDNIDEEAL HQIWSRCRAN YFVRHSPNQL AWHARHLLQH DLSKPLVLLS 700
PQATRGGTEI FIWSPDRPYL FAAVCAELDR RNLSVHDAQI FTTRDGMAMD 750
TFIVLEPDGS PLSADRHEVI RFGLEQVLTQ SSWQPPQPRR QPAKLRHFTV 800
ETEVTFLPTH TDRKSFLELI ALDQPGLLAR VGKIFADLGI SLHGARITTI 850
GERVEDLFII ATADRRALNN ELQQEVHQRL TEALNPNDKG 890
Length:890
Mass (Da):102,408
Last modified:September 5, 2006 - v1
Checksum:i8548A4598CE31A70
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000247 Genomic DNA. Translation: ABG68215.1.
RefSeqiYP_668114.1. NC_008253.1.

Genome annotation databases

EnsemblBacteriaiABG68215; ABG68215; ECP_0175.
GeneIDi4190257.
KEGGiecp:ECP_0175.
PATRICi18190991. VBIEscCol77757_0179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000247 Genomic DNA. Translation: ABG68215.1 .
RefSeqi YP_668114.1. NC_008253.1.

3D structure databases

ProteinModelPortali Q0TLG6.
SMRi Q0TLG6. Positions 469-599.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 362663.ECP_0175.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABG68215 ; ABG68215 ; ECP_0175 .
GeneIDi 4190257.
KEGGi ecp:ECP_0175.
PATRICi 18190991. VBIEscCol77757_0179.

Phylogenomic databases

eggNOGi COG2844.
HOGENOMi HOG000261778.
KOi K00990.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci ECOL362663:GIY5-173-MONOMER.

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

  1. "Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
    Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
    Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 536 / UPEC.

Entry informationi

Entry nameiGLND_ECOL5
AccessioniPrimary (citable) accession number: Q0TLG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: July 9, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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