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A9LZ86 (GLND_NEIM0) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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:

  1. [Protein-PII] uridylyltransferase
    Short name=PII uridylyltransferase
    Short name=UTase
    EC=2.7.7.59
  2. [Protein-PII]-UMP uridylyl-removing enzyme
    Short name=UR
    EC=3.1.4.-
Gene names
Name:glnD
Ordered Locus Names:NMCC_1086
OrganismNeisseria meningitidis serogroup C (strain 053442) [Complete proteome] [HAMAP]
Taxonomic identifier374833 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length852 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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. HAMAP-Rule MF_00277

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII]. HAMAP-Rule MF_00277

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII]. HAMAP-Rule MF_00277

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00277

Enzyme regulation

Uridylyltransferase (UTase) activity is inhibited by glutamine, while glutamine activates uridylyl-removing (UR) activity By similarity. HAMAP-Rule MF_00277

Domain

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. HAMAP-Rule MF_00277

Sequence similarities

Belongs to the GlnD family.

Contains 2 ACT domains.

Contains 1 HD domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 852852Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000078806

Regions

Domain437 – 539103HD
Domain673 – 75785ACT 1
Domain785 – 85268ACT 2
Region1 – 318318Uridylyltransferase HAMAP-Rule MF_00277
Region319 – 672354Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A9LZ86 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 6E3897F76ABFCCE0

FASTA85296,950
        10         20         30         40         50         60 
MPANLSSALE TFKRQRDAAE AHYLKANRVS VFFREYTAAV ETLLAALWVE HFQNSALCLM 

        70         80         90        100        110        120 
AVGGFGRGEL YPCSDVDLAV VSPAPLSDGI QEQIARFVQT LWDCKLMPSV KSGSVGELCE 

       130        140        150        160        170        180 
SVRDDITGDT AFLEARFLFG NRQTADELAK KMNAQRNVAA FVEAKLVEME HRHAKSQGSG 

       190        200        210        220        230        240 
AVLEPNIKSC PGGLRDIHTL LWIAKAQGLA TDLPDLLKQR ILTRAEAGML SHGYRRLAHI 

       250        260        270        280        290        300 
RIHLHLNAKR AEDRLLFDLQ PQVAESMGYE GLNLRRQSEE LMRVFYRAIK TVKQLGGILT 

       310        320        330        340        350        360 
PMLQSRVSST PLRVTLRIDD DYIQVNNQIA ARHTDIFFRR PEHIFKIVEI MQQRNDITAL 

       370        380        390        400        410        420 
EPQTLRAWWG ATRKINRSFY QNSENRHRFA GFFRNGNGLT QTLRFLNLYG VLGRYLPAWE 

       430        440        450        460        470        480 
KIVGLLQHDL FHIYPVDDHI LTVVRNVRRL ALDMHSHELP YASALMQSFE KQDILYLAAF 

       490        500        510        520        530        540 
FHDIAKGRGG DHAIQGIADA RQFAADHFLT EEESDLLAWL VENHLLMSTV AQKEDIQDPS 

       550        560        570        580        590        600 
VLDAFCKRVQ THERLSALYL LTISDIRGTN PKLWNAWRAS LLESLFHAAG RYLTGNGGNP 

       610        620        630        640        650        660 
HTLFGRRRQE AADLLTRAAV PEKQQKKLWN ALGSAYFARH QSREILWHAA NLVHDFETPI 

       670        680        690        700        710        720 
VRSRILPQSD SFQVMVFMPN GPRLFARLCR IFSRHGFDIL AARAFITEHD YILDTFIVQI 

       730        740        750        760        770        780 
PSQHAPEDYP DIQSALEAEL NSFIHGHTVA EISSHSRRIS RRSRYMPIAP SITITPEEDY 

       790        800        810        820        830        840 
PDWYSVEITA VNRPFLLADM AEVFFAHNVS LRYAKISTLD ERAEDSFTVF SPDLNNPKIQ 

       850 
SSLKQTLLEQ LS 

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References

[1]"Characterization of ST-4821 complex, a unique Neisseria meningitidis clone."
Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z., Liang X., Xu J., Jin Q.
Genomics 91:78-87(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 053442.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000381 Genomic DNA. Translation: ABX73263.1.
RefSeqYP_001599219.1. NC_010120.1.

3D structure databases

ProteinModelPortalA9LZ86.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374833.NMCC_1086.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX73263; ABX73263; NMCC_1086.
GeneID5796239.
KEGGnmn:NMCC_1086.
PATRIC20346794. VBINeiMen117761_1313.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMALYCLWDM.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BioCycNMEN374833:GJ7Z-1084-MONOMER.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
HAMAPMF_00277. PII_uridylyl_transf.
InterProIPR002912. ACT_dom.
IPR010043. GlnD_Uridyltrans.
IPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamPF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
[Graphical view]
PIRSFPIRSF006288. PII_uridyltransf. 1 hit.
SMARTSM00471. HDc. 1 hit.
[Graphical view]
TIGRFAMsTIGR01693. UTase_glnD. 1 hit.
PROSITEPS51671. ACT. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLND_NEIM0
AccessionPrimary (citable) accession number: A9LZ86
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: June 11, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families