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Q57T41

- GLND_SALCH

UniProt

Q57T41 - GLND_SALCH

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, SCH_0214
Organism
Salmonella choleraesuis (strain SC-B67)
Status
Reviewed - Annotation score: 3 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

BioCyciSENT321314:GJCS-221-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:SCH_0214
OrganismiSalmonella choleraesuis (strain SC-B67)
Taxonomic identifieri321314 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
ProteomesiUP000000538: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 890890Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_0000192763Add
BLAST

Proteomic databases

PaxDbiQ57T41.

Interactioni

Protein-protein interaction databases

STRINGi321314.SC0214.

Structurei

3D structure databases

ProteinModelPortaliQ57T41.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini468 – 601134HDAdd
BLAST
Domaini709 – 78476ACT 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.
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.

Q57T41-1 [UniParc]FASTAAdd to Basket

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MNTHPEQHAN TALPTLPDQP QNPGVWPRAE LTVAGIKARI DIFQHWLGEA    50
FDSGICAEQL IEARTEFIDQ LLQRLWIEAG FGQIADLALV AVGGYGRGEL 100
HPLSDIDLLI LSRKKLPDEQ AQKVGELLTL LWDVKLDVGH SVRTLEECLL 150
EGLSDLTVAT NLIETRLLIG DVALFLALQK HIFSEGFWPS DKFYAAKVEE 200
QNQRHQRYHG TSYNLEPDIK SSPGGLRDIH TLQWVARRHF GATSLDEMVG 250
FGFLTPAERA ELNECLHILW RIRFALHLVV SRYDNRLLFD RQLSVAQRLN 300
YSGEGNDPVE RMMKDYFRVT RRVSELNQML LQLFDEAILA LPADEKPRPV 350
DDEFQLRGTL IDLRDDTLFI REPQAILRMF YMMVRNSAIT GIYSTTLRHL 400
RHARRHLSQP LCYIPEARTL FLSMLRHPGA VSRGLLPMHR HSVLWAYMPQ 450
WSHIVGQMQF DLFHAYTVDE HTIRVMLKLE SFAKEETRQR HPLCVDLWPR 500
LPHPELILIA ALFHDIAKGR GGDHSVLGAQ DVLTFAELHG LNSRETQLVA 550
WLVRQHLLMS VTAQRRDIQD PEVIKQFAEE VQTETRLRFL VCLTVADICA 600
TNETLWNSWK QSLLRELYFA TEKQLRRGMQ NTPDMRERVR HHQLQALALL 650
RMDNIDEAAL HKIWTRCRAN YFVRHSPNQL AWHARHLLQH DLRQPLVLLS 700
PQATRGGTEI FIWSPDRPYL FAAVCAELDR RNLSVHDAQI FTTRDGMAMD 750
TFIVLEPDGS PLAADRHDVI RTGLEQTITQ RSWQPPQPRR QPAKLRHFTV 800
ETEVNFLPTH TDRKSFMELI ALDQPGLLAR VGQIFADLGI SLHGARITTI 850
GERVEDLFII ATADRRALNN VLQLEVQQRL TAAFNPNDKG 890
Length:890
Mass (Da):102,322
Last modified:May 10, 2005 - v1
Checksum:i5DDBF86CE67E1E44
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017220 Genomic DNA. Translation: AAX64120.1.
RefSeqiWP_001539051.1. NC_006905.1.
YP_215201.1. NC_006905.1.

Genome annotation databases

EnsemblBacteriaiAAX64120; AAX64120; SCH_0214.
PATRICi32320876. VBISalEnt136302_0465.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE017220 Genomic DNA. Translation: AAX64120.1 .
RefSeqi WP_001539051.1. NC_006905.1.
YP_215201.1. NC_006905.1.

3D structure databases

ProteinModelPortali Q57T41.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 321314.SC0214.

Proteomic databases

PaxDbi Q57T41.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAX64120 ; AAX64120 ; SCH_0214 .
PATRICi 32320876. VBISalEnt136302_0465.

Phylogenomic databases

eggNOGi COG2844.
OMAi HHLLMSV.
OrthoDBi EOG6CCH44.

Enzyme and pathway databases

BioCyci SENT321314:GJCS-221-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. "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen."
    Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S.
    Nucleic Acids Res. 33:1690-1698(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC-B67.

Entry informationi

Entry nameiGLND_SALCH
AccessioniPrimary (citable) accession number: Q57T41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: May 10, 2005
Last modified: September 3, 2014
This is version 67 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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