Skip Header

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

Q2Y5Q1

- GLND_NITMU

UniProt

Q2Y5Q1 - GLND_NITMU

(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

Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849)
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

Magnesium.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

BioCyciNMUL323848:GKEC-2679-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:Nmul_A2633
OrganismiNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849)
Taxonomic identifieri323848 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira
ProteomesiUP000002718: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 887887Bifunctional uridylyltransferase/uridylyl-removing enzymePRO_0000231684Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi323848.Nmul_A2633.

Structurei

3D structure databases

ProteinModelPortaliQ2Y5Q1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini448 – 555108HDUniRule annotationAdd
BLAST
Domaini687 – 77286ACT 1UniRule annotationAdd
BLAST
Domaini796 – 87176ACT 2UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 329329UridylyltransferaseAdd
BLAST
Regioni330 – 686357Uridylyl-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. 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.

Q2Y5Q1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKGLNAKPFS HEAVRQKLLS GRESLQRRYH QNRNGAALLR DHSRLVDGIL
60 70 80 90 100
RQVWHEMNMP GSTALLAVGG YGRRQLFPYS DIDLVVLLPD KGDAAEAMDN
110 120 130 140 150
ELGTRLEHWV GLLWDIGLDI GHSVRTVKEC GEEAANDITV QTSLLEARLL
160 170 180 190 200
GGNSDLFDRF LQVMETMLAP RKFFVDKQLE QQQRHKRYQD APYKLEPNIK
210 220 230 240 250
ESPGGLRDLQ NVLWISRAAG FGKTWSELAK KGFIIRREAR LIQRQQTVLQ
260 270 280 290 300
DLRIRLHYLG GRREDRLLFD YQNPLAEELG IAAKPPRRPG EMLMQRYYRA
310 320 330 340 350
ARSVTQVNTI LLLTLHAEIF PDEEAVTTII NERFQKRGDL LEICEEDIFE
360 370 380 390 400
RDPGAILESV LLLQQNPDLK GRSFATLRAM WRSAPLITAS FRREPRHCAM
410 420 430 440 450
FMEILRQPRG LTRELRLMNR YGILGRYIPA FGRIIGQMQH DLFHVYTVDE
460 470 480 490 500
HILMVVRNLR RFMAPEFAYE YPLCSRLINE FERPELLYLA GLFHDIAKGR
510 520 530 540 550
QGDHSLLGKV DARRFCERHR MPAEDTELVV WLVENHLHMS ATAQKKDIAD
560 570 580 590 600
AEVIADFAAS MRDERHLIAL YLLTVSDIRG TSPKVWNAWK GKLLEDLFHR
610 620 630 640 650
TRQYLCGETA LTDISLENRK NKVLQLLHPD DAAMRAYERF WSGLDSSYLM
660 670 680 690 700
MHDPREIAWH TQHLSQRMKS PAPIVKTRAA ETGAGVEVLV YTADQKDLFA
710 720 730 740 750
RICSFFDGID YNIVQAKIHT TREGYALDSF LVLDPFNVAN HDPREFQFIE
760 770 780 790 800
QELTQQLEQQ ALMATPVKGR LSRHLRHFPI TPQVSIEPDD SGAYYVLSIT
810 820 830 840 850
AGDQSGLLSR IAQVLVRFGL NVHSARINTL GERAEDTFLV TGSILSNSRS
860 870 880
VIQLEANLIK VLHTSPQPET PGKAPGKPSA GDRIIPR
Length:887
Mass (Da):101,510
Last modified:December 20, 2005 - v1
Checksum:iE65E0364AA37D84B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000103 Genomic DNA. Translation: ABB75920.1.
RefSeqiYP_413312.1. NC_007614.1.

Genome annotation databases

EnsemblBacteriaiABB75920; ABB75920; Nmul_A2633.
GeneIDi3786336.
KEGGinmu:Nmul_A2633.
PATRICi22729016. VBINitMul110821_3056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000103 Genomic DNA. Translation: ABB75920.1 .
RefSeqi YP_413312.1. NC_007614.1.

3D structure databases

ProteinModelPortali Q2Y5Q1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 323848.Nmul_A2633.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABB75920 ; ABB75920 ; Nmul_A2633 .
GeneIDi 3786336.
KEGGi nmu:Nmul_A2633.
PATRICi 22729016. VBINitMul110821_3056.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NMUL323848:GKEC-2679-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. "Complete sequence of chromosome 1 of Nitrosospira multiformis ATCC 25196."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25196 / NCIMB 11849.

Entry informationi

Entry nameiGLND_NITMU
AccessioniPrimary (citable) accession number: Q2Y5Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 20, 2005
Last modified: October 29, 2014
This is version 62 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3