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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Xanthomonas campestris pv. campestris (strain B100)
Status
Reviewed-Annotation score: 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.UniRule annotation

Catalytic activityi

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

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciXCAM509169:GHW4-2976-MONOMER.

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:xcc-b100_2914
OrganismiXanthomonas campestris pv. campestris (strain B100)
Taxonomic identifieri509169 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000001188 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 869869Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_1000114769Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB0RW57.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini451 – 570120HDUniRule annotationAdd
BLAST
Domaini692 – 77180ACT 1UniRule annotationAdd
BLAST
Domaini798 – 86972ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 332332UridylyltransferaseAdd
BLAST
Regioni333 – 691359Uridylyl-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.UniRule 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.
KOiK00990.
OMAiHTLFWIA.
OrthoDBiEOG6CCH44.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
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.

B0RW57-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTATPADRPD PGVAGDADWA AEARPLLVHA DMRLCKRFDQ GEPTERLLAL
60 70 80 90 100
RARAVDQLMR NAWARCIPAD ARLSLHAVGG YGRGELFPRS DVDLLVLGET
110 120 130 140 150
AAQQRHEQAL ARLFALLWDV GLPISHAVRS PAQCTSAAAD QTVLTALIES
160 170 180 190 200
RPLVADAQAR AALAAAIAPQ QVWPPRAFFQ AKREELHARH QRFGDTADNL
210 220 230 240 250
EPDIKDGPGG LRDLQTLGWM ALRAFGVKDL EALVGLGHVG MDEAAALRRE
260 270 280 290 300
REELARLRYG LHLVANRPEE RLRFDYQKTL AERLGFADDP ESLGVEKMMQ
310 320 330 340 350
RFYRSAALIR RISDRLLQRF EEQFDGEAVP VQLDAGFSLR RGYLTADADT
360 370 380 390 400
WPDGDVVQVF ALFAQWAAHR EVRGLHSLTA RALAEVLRDL PAYDVADAIA
410 420 430 440 450
RDRFMALLRG PRAVETLNRM ARLGVLGQWI PAFASVSGRM QFDLFHVYTV
460 470 480 490 500
DQHTLMVLRN IALFAAGRAD ERFSITHEVW PRLRKPELLL LAGLFHDIAK
510 520 530 540 550
GRGGDHSELG AVDARAFCLA HRLSEGDTEL VTWLVEQHLR MSVTAQKQDI
560 570 580 590 600
SDPEVIHRFA TLVGTRERLD YLYLLTCADI AGTSPKLWNA WKDRLLADLY
610 620 630 640 650
FAARRALREG LEHPPPREER LREARESART LMQAQGHDDA TIDRQFAGMP
660 670 680 690 700
DENFLRFRPE QLAWQAASLI EVQIGQTLVK ARRAVPDNDA LEVFVYSPDR
710 720 730 740 750
DGLFSAIVAT LDRKGYGIHR ARVLDAPHDA IFDVFEVLPQ DSSADGDPQR
760 770 780 790 800
LAAALRQVLA GDLLKVRPSR RAVPRQLRHF RFAPRVEFSE SAGGRRTRIS
810 820 830 840 850
LVAPDRPGLL ADVAHVLRMQ HLRVHDARIA TFGERAEDQF QITDEHDRPL
860
PDAARQALRD ALCACLDPT
Length:869
Mass (Da):97,315
Last modified:April 8, 2008 - v1
Checksum:i54BBE78E676E3BDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920689 Genomic DNA. Translation: CAP52275.1.

Genome annotation databases

EnsemblBacteriaiCAP52275; CAP52275; xcc-b100_2914.
KEGGixca:xccb100_2914.
PATRICi24085734. VBIXanCam108527_2945.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM920689 Genomic DNA. Translation: CAP52275.1.

3D structure databases

ProteinModelPortaliB0RW57.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAP52275; CAP52275; xcc-b100_2914.
KEGGixca:xccb100_2914.
PATRICi24085734. VBIXanCam108527_2945.

Phylogenomic databases

eggNOGiCOG2844.
KOiK00990.
OMAiHTLFWIA.
OrthoDBiEOG6CCH44.

Enzyme and pathway databases

BioCyciXCAM509169:GHW4-2976-MONOMER.

Family and domain databases

Gene3Di1.10.3210.10. 1 hit.
HAMAPiMF_00277. PII_uridylyl_transf.
InterProiIPR002912. ACT_dom.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
IPR010043. UTase/UR.
[Graphical view]
PfamiPF01842. ACT. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

  1. "The genome of Xanthomonas campestris pv. campestris B100 and its use for the reconstruction of metabolic pathways involved in xanthan biosynthesis."
    Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T., Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K., Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K., Puehler A.
    J. Biotechnol. 134:33-45(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: B100.

Entry informationi

Entry nameiGLND_XANCB
AccessioniPrimary (citable) accession number: B0RW57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: July 22, 2015
This is version 57 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.