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A5U6S3 (GLND_MYCTA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 56. 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:MRA_2943
OrganismMycobacterium tuberculosis (strain ATCC 25177 / H37Ra) [Complete proteome] [HAMAP]
Taxonomic identifier419947 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length808 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 – 808808Bifunctional uridylyltransferase/uridylyl-removing enzyme HAMAP-Rule MF_00277
PRO_1000022346

Regions

Domain431 – 536106HD
Domain610 – 68677ACT 1
Domain730 – 80576ACT 2
Region1 – 315315Uridylyltransferase HAMAP-Rule MF_00277
Region316 – 609294Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
A5U6S3 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 9B1F14D01C29F0B0

FASTA80886,438
        10         20         30         40         50         60 
MEAESPCAAS DLAVARRELL SGNHRELDPV GLRQTWLDLH ESWLIDKADE IGIADASGFA 

        70         80         90        100        110        120 
IVGVGGLGRR ELLPYSDLDV LLLHDGKPAD ILRPVADRLW YPLWDANIRL DHSVRTVSEA 

       130        140        150        160        170        180 
LTIANSDLMA ALGMLEARHI AGDQQLSFAL IDGVRRQWRN GIRSRMGELV EMTYARWRRC 

       190        200        210        220        230        240 
GRIAQRAEPD LKLGRGGLRD VQLLDALALA QLIDRHGIGH TDLPAGSLDG AYRTLLDVRT 

       250        260        270        280        290        300 
ELHRVSGRGR DHLLAQFADE ISAALGFGDR FDLARTLSSA GRTIGYHAEA GLRTAANALP 

       310        320        330        340        350        360 
RRGISALVRR PKRRPLDEGV VEYAGEIVLA RDAEPEHDPG LVLRVAAASA DTGLPIGAAT 

       370        380        390        400        410        420 
LSRLAASVPD LPTPWPQEAL DDLLVVLSAG PTTVATIEAL DRTGLWGRLL PEWEPIRDLP 

       430        440        450        460        470        480 
PRDVAHKWTV DRHVVETAVH AAPLATRVAR PDLLALGALL HDIGKGRGTD HSVLGAELVI 

       490        500        510        520        530        540 
PVCTRLGLSP PDVRTLSKLV RHHLLLPITA TRRDLNDPKT IEAVSEALGG DPQLLEVLHA 

       550        560        570        580        590        600 
LSEADSKATG PGVWSDWKAS LVDDLVRRCR MVMAGESLPQ AEPTAPHYLS LAADHGVHVE 

       610        620        630        640        650        660 
ISPRDGERID AVIVAPDERG LVSKAAAVLA LNSLRVHSAS VNVHQGVAIT EFVVSPLFGS 

       670        680        690        700        710        720 
PPAAELVRQQ FVGALNGDVD VLGMLQKRDS DAASLVSARA GDVQAGVPVT RTAAPPRILW 

       730        740        750        760        770        780 
LDTAAPAKLI LEVRAMDRAG LLALLAGALE GAGAGIVWAK VNTFGSTAAD VFCVTVPAEL 

       790        800 
DARAAVEQHL LEVLGASVDV VVDEPVGD 

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References

[1]"Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, a non-pathogenic variant closely related to the well-characterized pathogenic strain H37Rv."
Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25177 / H37Ra.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000611 Genomic DNA. Translation: ABQ74723.1.
RefSeqYP_001284285.1. NC_009525.1.

3D structure databases

ProteinModelPortalA5U6S3.
SMRA5U6S3. Positions 424-545, 605-655.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING419947.MRA_2943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ74723; ABQ74723; MRA_2943.
GeneID5215487.
KEGGmra:MRA_2943.
PATRIC18146209. VBIMycTub106795_3293.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000021840.
KOK00990.
OMAELREPWP.
OrthoDBEOG6CCH44.
ProtClustDBPRK03381.

Enzyme and pathway databases

BioCycMTUB419947:GJ8N-3043-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]
PfamPF01842. ACT. 1 hit.
PF08335. 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_MYCTA
AccessionPrimary (citable) accession number: A5U6S3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: March 19, 2014
This is version 56 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