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Q9X706 (GLND_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. 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:Cgl2059, cg2258
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length692 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.

Catalytic activity

UTP + [protein-PII] = diphosphate + uridylyl-[protein-PII].

Uridylyl-[protein-PII] + H2O = UMP + [protein-PII].

Cofactor

Magnesium By similarity.

Enzyme regulation

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

Domain

Has two distinct domains: an N-terminal nucleotidyltransferase (NT) domain responsible for UTase activity, and a HD domain that encodes UR activity By similarity. Lacks the two C-terminal ACT domains found in GlnD orthologs, that seem to have a role in glutamine sensing.

Sequence similarities

Belongs to the GlnD family.

Contains 1 HD domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 692692Bifunctional uridylyltransferase/uridylyl-removing enzyme
PRO_0000192730

Regions

Domain384 – 47491HD
Region1 – 270270Uridylyltransferase
Region271 – 692422Uridylyl-removing

Sequences

Sequence LengthMass (Da)Tools
Q9X706 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A7AC19614C133676

FASTA69275,970
        10         20         30         40         50         60 
MNNPAQLRQD TEKEVLALLG SLVLPAGTAL AATGSLARSE LTPYSDLDLI LIHPPGATPD 

        70         80         90        100        110        120 
GVEDLWYPIW DAKKRLDYSV RTPDECVAMI SADSTAALAM LDLRFVAGDE DLCAKTRRRI 

       130        140        150        160        170        180 
VEKWRQELNK NFDAVVDTAI ARWRRSGPVV AMTRPDLKHG RGGLRDFELI KALALGHLCN 

       190        200        210        220        230        240 
LPQLDAQHQL LLDARTLLHV HARRSRDVLD PEFAVDVAMD LGFVDRYHLG REIADAARAI 

       250        260        270        280        290        300 
DDGLTTALAT ARGILPRRTG FAFRNASRRP LDLDVVDANG TIELSKKPDL NDPALPLRVA 

       310        320        330        340        350        360 
AAAATTGLPV AESTWVRLNE CPPLPEPWPA NAAGDFFRIL SSPKNSRRVV KNMDRHGLWS 

       370        380        390        400        410        420 
RFVPEWDRIK GLMPREPSHI STIDEHSLNT VAGCALETVT VARPDLLVLG ALYHDIGKGF 

       430        440        450        460        470        480 
PRPHEQVGAE MVARAASRMG LNLRDRASVQ TLVAEHTAVA KIAARLDPSS EGAVDKLLDA 

       490        500        510        520        530        540 
VRYDLVTLNL LEVLTEADAK ATGPGVWTAR LEHALRIVCK RARDRLTDIR PVAPMIAPRS 

       550        560        570        580        590        600 
EIGLVERDGV FTVQWHGEDL HRILGVIYAK GWTITAARML ANGQWSAEFD VRANGPQDFD 

       610        620        630        640        650        660 
PQHFLQAYQS GVFSEVPIPA LGITATFWHG NTLEVRTELR TGAIFALLRT LPDALWINAV 

       670        680        690 
TRGATLIIQA ALKPGFDRAT VERSVVRSLA GS 

« Hide

References

« Hide 'large scale' references
[1]"Nitrogen regulation in Corynebacterium glutamicum: isolation of genes involved and biochemical characterization of corresponding proteins."
Jakoby M.J., Kraemer R., Burkovski A.
FEMS Microbiol. Lett. 173:303-310(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ010319 Genomic DNA. Translation: CAB39374.1.
BA000036 Genomic DNA. Translation: BAB99452.1.
BX927154 Genomic DNA. Translation: CAF20397.1.
RefSeqNP_601262.1. NC_003450.3.
YP_226298.1. NC_006958.1.

3D structure databases

ProteinModelPortalQ9X706.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg2258.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB99452; BAB99452; BAB99452.
CAF20397; CAF20397; cg2258.
GeneID1020013.
KEGGcgb:cg2258.
cgl:NCgl1981.
PATRIC21496122. VBICorGlu203724_1997.

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000021840.
KOK00990.
OMAGCALETV.
OrthoDBEOG6CCH44.

Enzyme and pathway databases

BRENDA2.7.7.59. 1648.

Family and domain databases

Gene3D1.10.3210.10. 1 hit.
InterProIPR003607. HD/PDEase_dom.
IPR006674. HD_domain.
IPR002934. Nucleotidyltransferase.
IPR013546. PII_UdlTrfase/GS_AdlTrfase.
[Graphical view]
PfamPF08335. GlnD_UR_UTase. 1 hit.
PF01966. HD. 1 hit.
PF01909. NTP_transf_2. 1 hit.
[Graphical view]
SMARTSM00471. HDc. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLND_CORGL
AccessionPrimary (citable) accession number: Q9X706
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 89 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