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A9R397

- GLND_YERPG

UniProt

A9R397 - GLND_YERPG

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, YpAngola_A3437
Organism
Yersinia pestis bv. Antiqua (strain Angola)
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

BioCyciYPES349746:GHPB-3448-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:YpAngola_A3437
OrganismiYersinia pestis bv. Antiqua (strain Angola)
Taxonomic identifieri349746 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
ProteomesiUP000001204: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 893893Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000114770Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi349746.YpAngola_A3437.

Structurei

3D structure databases

ProteinModelPortaliA9R397.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini470 – 603134HDAdd
BLAST
Domaini711 – 79383ACT 1Add
BLAST
Domaini819 – 89375ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 351351UridylyltransferaseUniRule annotationAdd
BLAST
Regioni352 – 710359Uridylyl-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.

A9R397-1 [UniParc]FASTAAdd to Basket

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MSDNHTEHSL SLTLTPTISE QPALPSTYLD SDIHCPILKQ RLDAFQRWQA    50
EAFNSGTSAE VLIAARSDYI DHLLQRLWTF YGFDKVPETA LVAVGGYGRG 100
ELHPLSDIDV LVLSKQRLND EQAQRVGQLI TLLWDLKLEV GHSVRTLEEC 150
LLEGLADLTI ATNMIESRLI CGDVALFLQM QKHIFSDSFW PSPQFFHAKV 200
VEQQERHKRY HGTSYNLEPD IKSSPGGLRD IHTLLWVARR HFGATSLSEM 250
VDFGFLTNAE RNELNESQSF LWRIRFALHL VLTRYDNRLL FDRQLSVAQL 300
LRYEGEGNEP VEHMMKDFYR MTRRVSELNN MLLQLFDEAI LALDANEKPR 350
PLDEEFQLRG DLIDLRDENL FVRQPEAIMR MFYLMVRNQD IKGIYSTTVR 400
RLRHARRHLK APLCHIPEAR KLFMAILRHP GAVSRALLPM HRHSVLWAYM 450
PQWGSIVGQM QFDLFHAYTV DEHTIRVLLK IESFADEDTR PRHPLCVELY 500
PRLPQPELLL LAALFHDIAK GRGGDHSILG AHDAVEFAEQ HGLNSRESQL 550
VAWLVRCHLL MSVTAQRRDI QDPAVIQQFS AEVQSETRLR YLVSLTVADI 600
CATNENLWNS WKQSLLRELY FATEKQLRRG MQNSPDLRER VRHHRLQALA 650
LLRMDNIDEE ALHRIWSRCR ADYFLRHSPN QLAWHARHLL EHDSTKPLVL 700
VSRQATRGGT EIFIWSPDRP SLFAAVVGEL DRRNLSVHDA QIFTNRDGMA 750
MDTFIVLEPD GSPLAQDRHP IISHALQQAI NRSDYQHPPR VRRLSPKLRH 800
FSVPTEANFL PTHNERRTYL ELIALDQPGL LARVGKIFAD LGLSLHSARI 850
TTIGERVEDL FVLADKDRRA LSLETRRELA QRLADTLNPN DKL 893
Length:893
Mass (Da):103,158
Last modified:February 5, 2008 - v1
Checksum:iAE09A7808DB3D611
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX88111.1.
RefSeqiYP_001607773.1. NC_010159.1.

Genome annotation databases

EnsemblBacteriaiABX88111; ABX88111; YpAngola_A3437.
GeneIDi5801914.
KEGGiypg:YpAngola_A3437.
PATRICi18576521. VBIYerPes97331_4015.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000901 Genomic DNA. Translation: ABX88111.1 .
RefSeqi YP_001607773.1. NC_010159.1.

3D structure databases

ProteinModelPortali A9R397.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 349746.YpAngola_A3437.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABX88111 ; ABX88111 ; YpAngola_A3437 .
GeneIDi 5801914.
KEGGi ypg:YpAngola_A3437.
PATRICi 18576521. VBIYerPes97331_4015.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci YPES349746:GHPB-3448-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. "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
    Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
    J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Angola.

Entry informationi

Entry nameiGLND_YERPG
AccessioniPrimary (citable) accession number: A9R397
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: June 11, 2014
This is version 51 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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