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B0VR80 (GLND_ACIBS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:ABSDF2174
OrganismAcinetobacter baumannii (strain SDF) [Complete proteome] [HAMAP]
Taxonomic identifier509170 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

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_1000114747

Regions

Domain492 – 58695HD
Domain700 – 78283ACT 1
Domain809 – 88779ACT 2
Region1 – 337337Uridylyltransferase HAMAP-Rule MF_00277
Region339 – 699361Uridylyl-removing HAMAP-Rule MF_00277

Sequences

Sequence LengthMass (Da)Tools
B0VR80 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 5BECB62B8B1D33F9

FASTA887102,102
        10         20         30         40         50         60 
MINTSPLLNY VSSHHDIKAI NQWRTDVEKQ LQDSYENGQS IREIIKARSD LVDEALVFLW 

        70         80         90        100        110        120 
KHAELDQSKL GLFAVGGYGR REMLPYSDVD IMILSEDEIS EENEKRISTF ISSLWDVGNF 

       130        140        150        160        170        180 
KPGISVRTIQ SCVEQAATDL TVATTLIEAR LITGNTQLAK WPRRIVSQTW TDKTFYDAKM 

       190        200        210        220        230        240 
AEQAKRYHQH NNTESNLEPD IKNAPGGIRD INQIGWIAKR HFRVNRIYDL VHLGFISEFE 

       250        260        270        280        290        300 
LAVLEEAESF LWEIRHHLHR LAKRDENRLL FDHQREIAAK FGYVRQEGQP VNYGVEQFMK 

       310        320        330        340        350        360 
RYYRTAQQVS TLNEMLLAYF SESVITPRLP NYERKIEVVN DHFKIVDNKI AVQHHKIFAE 

       370        380        390        400        410        420 
HPSAILELFY ILANRPDIEG IRARTLRLLI LAAKRINQSY RDNPEHQALF MSIIRSPYRL 

       430        440        450        460        470        480 
YDTLVAMKRY GVLGNYIPAF GQIMGLMQYD LFHIYTVDAH TLLLLRNLNR FREPEFAKEF 

       490        500        510        520        530        540 
PVVSSVFQRL ARQDIVFIAA LFHDIAKGRG GDHSELGAED AIEFGRAHGF TERECKLIAW 

       550        560        570        580        590        600 
LIQNHLLMSL TAQKKDISDP DVVKDFAEKL GDMEHLDYLY TLTVADINAT NPKLWNTWRA 

       610        620        630        640        650        660 
SLMRQLYTHA RDVIRTGLGR PVDYQMLIED TKFAASELLV NNFALADVEK VWQELGDEYF 

       670        680        690        700        710        720 
IKESADEIAW HTQAILKHGD NPEPLVLLRA HRKAAQDAVQ IFIYTRDQPN LFATTVAVLD 

       730        740        750        760        770        780 
RMNLDVQDAK IITASTAFSL DTYVVLDRFG TLLTDPEREE TVKNALVKAL SQPDQYPGLM 

       790        800        810        820        830        840 
QRRIPRQLRH FDIENTVDVT LNEALQQNMV EISTLDHPGL LARVGGLFMM QGLDIHSARI 

       850        860        870        880 
ATLGERAEDI FFVTKKDGKP LNNEEVKLFS EKLKAALDEA SNQICQH 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SDF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU468230 Genomic DNA. Translation: CAP01499.1.
RefSeqYP_001707469.1. NC_010400.1.

3D structure databases

ProteinModelPortalB0VR80.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509170.ABSDF2174.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAP01499; CAP01499; ABSDF2174.
GeneID5987229.
KEGGabm:ABSDF2174.
PATRIC20735117. VBIAciBau88365_2068.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2844.
HOGENOMHOG000261778.
KOK00990.
OMASPKVWNA.
OrthoDBEOG6CCH44.
ProtClustDBCLSK830629.

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_ACIBS
AccessionPrimary (citable) accession number: B0VR80
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 46 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