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A9R397

- GLND_YERPG

UniProt

A9R397 - GLND_YERPG

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene

glnD

Organism
Yersinia pestis bv. Antiqua (strain Angola)
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.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

  1. [protein-PII] uridylyltransferase activity Source: UniProtKB-HAMAP
  2. amino acid binding Source: InterPro
  3. 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 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: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 enzymePRO_1000114770Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi349746.YpAngola_A3437.

Structurei

3D structure databases

ProteinModelPortaliA9R397.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini470 – 603134HDUniRule annotationAdd
BLAST
Domaini711 – 79383ACT 1UniRule annotationAdd
BLAST
Domaini819 – 89375ACT 2UniRule annotationAdd
BLAST

Region

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

« Hide

        10         20         30         40         50
MSDNHTEHSL SLTLTPTISE QPALPSTYLD SDIHCPILKQ RLDAFQRWQA
60 70 80 90 100
EAFNSGTSAE VLIAARSDYI DHLLQRLWTF YGFDKVPETA LVAVGGYGRG
110 120 130 140 150
ELHPLSDIDV LVLSKQRLND EQAQRVGQLI TLLWDLKLEV GHSVRTLEEC
160 170 180 190 200
LLEGLADLTI ATNMIESRLI CGDVALFLQM QKHIFSDSFW PSPQFFHAKV
210 220 230 240 250
VEQQERHKRY HGTSYNLEPD IKSSPGGLRD IHTLLWVARR HFGATSLSEM
260 270 280 290 300
VDFGFLTNAE RNELNESQSF LWRIRFALHL VLTRYDNRLL FDRQLSVAQL
310 320 330 340 350
LRYEGEGNEP VEHMMKDFYR MTRRVSELNN MLLQLFDEAI LALDANEKPR
360 370 380 390 400
PLDEEFQLRG DLIDLRDENL FVRQPEAIMR MFYLMVRNQD IKGIYSTTVR
410 420 430 440 450
RLRHARRHLK APLCHIPEAR KLFMAILRHP GAVSRALLPM HRHSVLWAYM
460 470 480 490 500
PQWGSIVGQM QFDLFHAYTV DEHTIRVLLK IESFADEDTR PRHPLCVELY
510 520 530 540 550
PRLPQPELLL LAALFHDIAK GRGGDHSILG AHDAVEFAEQ HGLNSRESQL
560 570 580 590 600
VAWLVRCHLL MSVTAQRRDI QDPAVIQQFS AEVQSETRLR YLVSLTVADI
610 620 630 640 650
CATNENLWNS WKQSLLRELY FATEKQLRRG MQNSPDLRER VRHHRLQALA
660 670 680 690 700
LLRMDNIDEE ALHRIWSRCR ADYFLRHSPN QLAWHARHLL EHDSTKPLVL
710 720 730 740 750
VSRQATRGGT EIFIWSPDRP SLFAAVVGEL DRRNLSVHDA QIFTNRDGMA
760 770 780 790 800
MDTFIVLEPD GSPLAQDRHP IISHALQQAI NRSDYQHPPR VRRLSPKLRH
810 820 830 840 850
FSVPTEANFL PTHNERRTYL ELIALDQPGL LARVGKIFAD LGLSLHSARI
860 870 880 890
TTIGERVEDL FVLADKDRRA LSLETRRELA QRLADTLNPN DKL
Length:893
Mass (Da):103,158
Last modified:February 5, 2008 - v1
Checksum:iAE09A7808DB3D611
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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: November 26, 2014
This is version 54 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