SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

A8GIE8

- GLND_SERP5

UniProt

A8GIE8 - GLND_SERP5

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, Spro_3792
Organism
Serratia proteamaculans (strain 568)
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

BioCyciSPRO399741:GI55-3872-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:Spro_3792
OrganismiSerratia proteamaculans (strain 568)
Taxonomic identifieri399741 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia
ProteomesiUP000007074: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 892892Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_1000059226Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi399741.Spro_3792.

Structurei

3D structure databases

ProteinModelPortaliA8GIE8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini470 – 603134HDAdd
BLAST
Domaini711 – 79282ACT 1Add
BLAST
Domaini818 – 89275ACT 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.

A8GIE8-1 [UniParc]FASTAAdd to Basket

« Hide

MSENFRQQDT SVISPQAVPV QPEYPNAYGD EEINCIALKQ RLEQFQLWLA    50
AAFNAGSSAE SLVAARSDFI DRLLRRLWVF YGFEDIPETA LVAVGGYGRG 100
ELHPLSDIDV LVLSQRRLNE QQSQRVGEFI TLLWDLKLEV GHSVRTLEEC 150
LLEGLADLTV ATNLIESRMI CGDVALFLQM QKHIFSDGFW PSPQFFHAKV 200
VEQQERHQRY HGTSYNLEPD IKSSPGGLRD IHTLLWVARR HFGATSLDEM 250
VGFGFLTQAE RNELNECQSF LWRIRFALHL VLPRYDNRLL FDRQLNVAQL 300
LRYEGEGNEP VERMMKDFYR MTRRVGELNH MLLQLFDEAI LALDATEKPR 350
PLNDDFQLRG DLIDLRDETL FIRQPESIMR MFYLMVRNRE IKGIYSTTVR 400
QLRHARRHLK QPLCTIPEAR ELFMAILRHP GAVSRALVPM HRHSVLWAYM 450
PQWGKIVGQM QFDLFHAYTV DEHTIRVLQK LESFADAETR PRHPLCVELY 500
PRLPNPELLL LAALFHDIAK GRGGDHSILG AQDVLEFAEV HGLNSREAQL 550
VAWLVRCHLL MSVTAQRRDI QDPTVIQQFS AEVQSETRLR YLVCLTVADI 600
CATNETLWNS WKQSLLRELY FATEKQLRRG MQNSPDLRER VRHHRLQALA 650
LLRMDNIDEE ALHRIWSRCR ADYFLRHSPN QLAWHARHLL AHDSTKPLVL 700
VSRQATRGGT EIFIWSPDRP YLFAAVAGEM DRRNLSVHDA QIFTNRDGMA 750
MDTFIVLEPD GSPLAQDRHT AIRHALLQAI TQREYQPPRV RRPSSKLRHF 800
SVPTEVSFLP THTDRRSYLE LTALDQPGLL ARVGEVFADL NLSLHGARIS 850
TIGERVEDLF ILADSDRRAL NPETRRKLEQ RLTEALNPND KM 892
Length:892
Mass (Da):103,200
Last modified:November 13, 2007 - v1
Checksum:i8D6DC4E817EDB145
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000826 Genomic DNA. Translation: ABV42888.1.
RefSeqiYP_001480016.1. NC_009832.1.

Genome annotation databases

EnsemblBacteriaiABV42888; ABV42888; Spro_3792.
GeneIDi5607191.
KEGGispe:Spro_3792.
PATRICi32420400. VBISerPro44537_3852.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000826 Genomic DNA. Translation: ABV42888.1 .
RefSeqi YP_001480016.1. NC_009832.1.

3D structure databases

ProteinModelPortali A8GIE8.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 399741.Spro_3792.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABV42888 ; ABV42888 ; Spro_3792 .
GeneIDi 5607191.
KEGGi spe:Spro_3792.
PATRICi 32420400. VBISerPro44537_3852.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SPRO399741:GI55-3872-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 568.

Entry informationi

Entry nameiGLND_SERP5
AccessioniPrimary (citable) accession number: A8GIE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: June 11, 2014
This is version 50 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