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B0RW57

- GLND_XANCB

UniProt

B0RW57 - GLND_XANCB

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, xcc-b100_2914
Organism
Xanthomonas campestris pv. campestris (strain B100)
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

BioCyciXCAM509169:GHW4-2976-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:xcc-b100_2914
OrganismiXanthomonas campestris pv. campestris (strain B100)
Taxonomic identifieri509169 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas
ProteomesiUP000001188: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 869869Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000114769Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi509169.xccb100_2914.

Structurei

3D structure databases

ProteinModelPortaliB0RW57.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini451 – 570120HDAdd
BLAST
Domaini692 – 77180ACT 1Add
BLAST
Domaini798 – 86972ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 332332UridylyltransferaseUniRule annotationAdd
BLAST
Regioni333 – 691359Uridylyl-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.
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. 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

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MTATPADRPD PGVAGDADWA AEARPLLVHA DMRLCKRFDQ GEPTERLLAL    50
RARAVDQLMR NAWARCIPAD ARLSLHAVGG YGRGELFPRS DVDLLVLGET 100
AAQQRHEQAL ARLFALLWDV GLPISHAVRS PAQCTSAAAD QTVLTALIES 150
RPLVADAQAR AALAAAIAPQ QVWPPRAFFQ AKREELHARH QRFGDTADNL 200
EPDIKDGPGG LRDLQTLGWM ALRAFGVKDL EALVGLGHVG MDEAAALRRE 250
REELARLRYG LHLVANRPEE RLRFDYQKTL AERLGFADDP ESLGVEKMMQ 300
RFYRSAALIR RISDRLLQRF EEQFDGEAVP VQLDAGFSLR RGYLTADADT 350
WPDGDVVQVF ALFAQWAAHR EVRGLHSLTA RALAEVLRDL PAYDVADAIA 400
RDRFMALLRG PRAVETLNRM ARLGVLGQWI PAFASVSGRM QFDLFHVYTV 450
DQHTLMVLRN IALFAAGRAD ERFSITHEVW PRLRKPELLL LAGLFHDIAK 500
GRGGDHSELG AVDARAFCLA HRLSEGDTEL VTWLVEQHLR MSVTAQKQDI 550
SDPEVIHRFA TLVGTRERLD YLYLLTCADI AGTSPKLWNA WKDRLLADLY 600
FAARRALREG LEHPPPREER LREARESART LMQAQGHDDA TIDRQFAGMP 650
DENFLRFRPE QLAWQAASLI EVQIGQTLVK ARRAVPDNDA LEVFVYSPDR 700
DGLFSAIVAT LDRKGYGIHR ARVLDAPHDA IFDVFEVLPQ DSSADGDPQR 750
LAAALRQVLA GDLLKVRPSR RAVPRQLRHF RFAPRVEFSE SAGGRRTRIS 800
LVAPDRPGLL ADVAHVLRMQ HLRVHDARIA TFGERAEDQF QITDEHDRPL 850
PDAARQALRD ALCACLDPT 869
Length:869
Mass (Da):97,315
Last modified:April 8, 2008 - v1
Checksum:i54BBE78E676E3BDF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM920689 Genomic DNA. Translation: CAP52275.1.
RefSeqiYP_001904319.1. NC_010688.1.

Genome annotation databases

EnsemblBacteriaiCAP52275; CAP52275; xcc-b100_2914.
GeneIDi6322903.
KEGGixca:xccb100_2914.
PATRICi24085734. VBIXanCam108527_2945.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM920689 Genomic DNA. Translation: CAP52275.1 .
RefSeqi YP_001904319.1. NC_010688.1.

3D structure databases

ProteinModelPortali B0RW57.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 509169.xccb100_2914.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAP52275 ; CAP52275 ; xcc-b100_2914 .
GeneIDi 6322903.
KEGGi xca:xccb100_2914.
PATRICi 24085734. VBIXanCam108527_2945.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci XCAM509169:GHW4-2976-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. 1 hit.
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 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: June 11, 2014
This is version 49 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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