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Q5F8H5

- GLND_NEIG1

UniProt

Q5F8H5 - GLND_NEIG1

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Protein

Bifunctional uridylyltransferase/uridylyl-removing enzyme

Gene
glnD, NGO0798
Organism
Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
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

BioCyciNGON242231:GI2G-752-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:NGO0798
OrganismiNeisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Taxonomic identifieri242231 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria
ProteomesiUP000000535: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzymeUniRule annotationPRO_0000192746Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi242231.NGO0798.

Structurei

3D structure databases

ProteinModelPortaliQ5F8H5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini437 – 539103HDAdd
BLAST
Domaini673 – 75785ACT 1Add
BLAST
Domaini785 – 85268ACT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 318318UridylyltransferaseUniRule annotationAdd
BLAST
Regioni319 – 672354Uridylyl-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.
OMAiLYCLWDM.
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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamiPF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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.

Q5F8H5-1 [UniParc]FASTAAdd to Basket

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MPENLSSALE TFKQQRNAAE AHYLKANRVS VFFREYTAAV ETLLAALWAE    50
HFQNSALCLM AVGGFGRGEP YPCSDVDLAV VSPAPLSDGI QEQIARFIQT 100
LWDCKLMPSV KSGSVDELCE SVRDDITGDT AFLEARFLFG NRQTADELAE 150
KMNVQRNVAA FIEAKLVEME HRHAKSQGSG AVLEPNIKSC PGGLRDIHTL 200
LWIAKAQGLA ANLPDLLKQR ILTRAEAGML SHGYRRLAHI RIRLHLNAKR 250
AEDRLLFDLQ PQVAESMGYQ DENRRRQSEE LMRVFYRAVK TVKQLGGILT 300
PMLRSRVSST PVRVTLRIDD DYIQVNNQIA ARHTDIFFRR PEHIFKIVEI 350
MQQRNDITAL EPQTLRAWWG ATRKINRSFY QNSENRRRFA GFFRSGNGLT 400
QTLRFLNLYG VLGRYLPAWE KIVGLLQHDL FHIYPVDDHI LAVVRNVRRL 450
ALDMHSHELP YASALMQSFE KQDILYLAAF FHDIAKGRGG DHAVQGIADA 500
RQFAADHFLT EEESDLLAWL VENHLLMSAV AQKEDIQDPG VLDAFCKRVQ 550
THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RCLAGNDGNP 600
HALFGRRRQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA 650
NLVHDFEPPI VRSRILPQSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL 700
AARAFITEHD YILDTFIVQI PSQHAPEDYP DIQSALEAEL NSFIHGHTVA 750
ETQSCNRRIS RRSRYMPIAP SITITPEEDY PDRYSVEITA VNRPFLLADM 800
AEVFFAHNVS LRYAKISTLD ERVEDSFTVF SPDLKNPKIQ SSLKQALLEQ 850
LA 852
Length:852
Mass (Da):96,964
Last modified:March 15, 2005 - v1
Checksum:i446EC476F5205885
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004969 Genomic DNA. Translation: AAW89512.1.
RefSeqiWP_010951127.1. NC_002946.2.
YP_207924.1. NC_002946.2.

Genome annotation databases

EnsemblBacteriaiAAW89512; AAW89512; NGO0798.
GeneIDi3282021.
KEGGingo:NGO0798.
PATRICi20334744. VBINeiGon24812_0944.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE004969 Genomic DNA. Translation: AAW89512.1 .
RefSeqi WP_010951127.1. NC_002946.2.
YP_207924.1. NC_002946.2.

3D structure databases

ProteinModelPortali Q5F8H5.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 242231.NGO0798.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW89512 ; AAW89512 ; NGO0798 .
GeneIDi 3282021.
KEGGi ngo:NGO0798.
PATRICi 20334744. VBINeiGon24812_0944.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci NGON242231:GI2G-752-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.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view ]
Pfami PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 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 complete genome sequence of Neisseria gonorrhoeae."
    Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F., Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C., Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H.
    , Qi S., Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.
    Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700825 / FA 1090.

Entry informationi

Entry nameiGLND_NEIG1
AccessioniPrimary (citable) accession number: Q5F8H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: March 15, 2005
Last modified: September 3, 2014
This is version 64 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

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