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Q2Y5Q1 (GLND_NITMU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:Nmul_A2633
OrganismNitrosospira multiformis (strain ATCC 25196 / NCIMB 11849) [Complete proteome] [HAMAP]
Taxonomic identifier323848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosospira

Protein attributes

Sequence length887 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 – 887887Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_0000231684

Regions

Domain448 – 555108HD
Domain687 – 77286ACT 1
Domain796 – 87176ACT 2
Region1 – 329329Uridylyltransferase HAMAP-Rule MF_00277
Region330 – 686357Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
Q2Y5Q1 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: E65E0364AA37D84B

FASTA887101,510
        10         20         30         40         50         60 
MKGLNAKPFS HEAVRQKLLS GRESLQRRYH QNRNGAALLR DHSRLVDGIL RQVWHEMNMP 

        70         80         90        100        110        120 
GSTALLAVGG YGRRQLFPYS DIDLVVLLPD KGDAAEAMDN ELGTRLEHWV GLLWDIGLDI 

       130        140        150        160        170        180 
GHSVRTVKEC GEEAANDITV QTSLLEARLL GGNSDLFDRF LQVMETMLAP RKFFVDKQLE 

       190        200        210        220        230        240 
QQQRHKRYQD APYKLEPNIK ESPGGLRDLQ NVLWISRAAG FGKTWSELAK KGFIIRREAR 

       250        260        270        280        290        300 
LIQRQQTVLQ DLRIRLHYLG GRREDRLLFD YQNPLAEELG IAAKPPRRPG EMLMQRYYRA 

       310        320        330        340        350        360 
ARSVTQVNTI LLLTLHAEIF PDEEAVTTII NERFQKRGDL LEICEEDIFE RDPGAILESV 

       370        380        390        400        410        420 
LLLQQNPDLK GRSFATLRAM WRSAPLITAS FRREPRHCAM FMEILRQPRG LTRELRLMNR 

       430        440        450        460        470        480 
YGILGRYIPA FGRIIGQMQH DLFHVYTVDE HILMVVRNLR RFMAPEFAYE YPLCSRLINE 

       490        500        510        520        530        540 
FERPELLYLA GLFHDIAKGR QGDHSLLGKV DARRFCERHR MPAEDTELVV WLVENHLHMS 

       550        560        570        580        590        600 
ATAQKKDIAD AEVIADFAAS MRDERHLIAL YLLTVSDIRG TSPKVWNAWK GKLLEDLFHR 

       610        620        630        640        650        660 
TRQYLCGETA LTDISLENRK NKVLQLLHPD DAAMRAYERF WSGLDSSYLM MHDPREIAWH 

       670        680        690        700        710        720 
TQHLSQRMKS PAPIVKTRAA ETGAGVEVLV YTADQKDLFA RICSFFDGID YNIVQAKIHT 

       730        740        750        760        770        780 
TREGYALDSF LVLDPFNVAN HDPREFQFIE QELTQQLEQQ ALMATPVKGR LSRHLRHFPI 

       790        800        810        820        830        840 
TPQVSIEPDD SGAYYVLSIT AGDQSGLLSR IAQVLVRFGL NVHSARINTL GERAEDTFLV 

       850        860        870        880 
TGSILSNSRS VIQLEANLIK VLHTSPQPET PGKAPGKPSA GDRIIPR 

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References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000103 Genomic DNA. Translation: ABB75920.1.
RefSeqYP_413312.1. NC_007614.1.

3D structure databases

ProteinModelPortalQ2Y5Q1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323848.Nmul_A2633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB75920; ABB75920; Nmul_A2633.
GeneID3786336.
KEGGnmu:Nmul_A2633.
PATRIC22729016. VBINitMul110821_3056.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBPRK03059.

Enzyme and pathway databases

BioCycNMUL323848:GKEC-2679-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.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PANTHERPTHR13734:SF1. PTHR13734:SF1. 1 hit.
PfamPF01842. ACT. 1 hit.
PF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 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_NITMU
AccessionPrimary (citable) accession number: Q2Y5Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: December 20, 2005
Last modified: February 19, 2014
This is version 58 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